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Journal articles on the topic 'Gly-met'

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Published: 4 June 2021
Last updated: 7 February 2022

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1

Lau, Justin Kai-Chi, Seydina Lo, Junfang Zhao, K. W. Michael Siu, and Alan C. Hopkinson. "Fragmentation Chemistry of [Met-Gly]•+, [Gly-Met]•+, and [Met-Met]•+ Radical Cations." Journal of The American Society for Mass Spectrometry 24, no. 4 (February 26, 2013): 543–53. http://dx.doi.org/10.1007/s13361-013-0581-5.

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2

Barata-Vallejo, Sebastian, Carla Ferreri, Tao Zhang, Hjalmar Permentier, Rainer Bischoff, Krzysztof Bobrowski, and Chryssostomos Chatgilialoglu. "Radiation chemical studies of Gly-Met-Gly in aqueous solution." Free Radical Research 50, sup1 (October 25, 2016): S24—S39. http://dx.doi.org/10.1080/10715762.2016.1231402.

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3

GUANTIERI, V., A. M. TAMBURRO, D. CABROL, H. BROCH, and D. VASILESCU. "Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro)." International Journal of Peptide and Protein Research 29, no. 2 (January 12, 2009): 216–30. http://dx.doi.org/10.1111/j.1399-3011.1987.tb02248.x.

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4

Morozova, Olga B., Sergey E. Korchak, Hans-Martin Vieth, and Alexandra V. Yurkovskaya. "Photo-CIDNP Study of Transient Radicals of Met-Gly and Gly-Met Peptides in Aqueous Solution at Variable pH." Journal of Physical Chemistry B 113, no. 20 (May 21, 2009): 7398–406. http://dx.doi.org/10.1021/jp8112182.

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5

Jannatul, Ferdouse, Yuki Kusaba, Yuki Fujimaru, Yuki Yamamoto, and Hiroshi Kitagaki. "Methionine and Glycine Stabilize Mitochondrial Activity in Sake Yeast During Ethanol Fermentation." Food technology and biotechnology 57, no. 4 (2019): 535–43. http://dx.doi.org/10.17113/ftb.57.04.19.5665.

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Addition of amino acids to fermentation media affects the growth and brewing profiles of yeast. In addition, retaining mitochondrial activity during fermentation is critical for the fermentation profiles of brewer’s yeasts. However, a concrete mechanism linking amino acids in fermentation media with mitochondrial activity during fermentation of brewer’s yeasts is yet unknown. Here, we report that amino acids in fermentation media, especially methionine (Met) and glycine (Gly), stabilize mitochondrial activity during fermentation of sake yeast. By utilizing atg32Δ mutant sake yeast, which shows deteriorated mitochondrial activity, we screened candidate amino acids that strengthened the mitochondrial activity of sake yeast during fermentation. We identified Met and Gly as candidate amino acids that fortify mitochondrial activity in sake yeast during fermentation. To confirm this biochemically, we measured reactive oxygen species (ROS) levels in sake yeast fermented with Met and Gly. Yeast cells supplemented with Met and Gly retained high ROS levels relative to the non-supplemented sake yeast. Moreover, Met-supplemented cells showed a metabolome distinct from that of non-supplemented cells. These results indicate that specific amino acids such as Met and Gly stabilize the mitochondrial activity of sake yeast during fermentation and thus manipulate brewing profiles of yeast.
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6

Yamane, T., Y. Shiraishi, and T. Ashida. "Structure of Boc-Pro-Met-Gly-OBzl, C24H35N3O6S." Acta Crystallographica Section C Crystal Structure Communications 41, no. 6 (June 15, 1985): 946–50. http://dx.doi.org/10.1107/s0108270185006138.

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7

Brinkworth, Craig S., Tara L. Pukala, John H. Bowie, and Michael J. Tyler. "Host Defence Peptides from the Skin Glands of Australian Amphibians. Caerulein Neuropeptides and Antimicrobial, Anticancer, and nNOS Inhibiting Citropins from the Glandular Frog Litoria subglandulosa." Australian Journal of Chemistry 57, no. 7 (2004): 693. http://dx.doi.org/10.1071/ch03325.

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The host defence peptides from the skin secretions of the Australian Glandular Frog (Litoria subglandulosa) are similar to those of the closely related species Litoria citropa. Both species produce several potent caerulein neuropeptides and antimicrobial- and anticancer-active citropin peptides. The major neuropeptides from Litoria subglandulosa are caerulein 1.1 [pGlu Gln Asp Tyr(SO3) Thr Gly Trp Met Asp Phe–NH2], caerulein 1.2 [pGlu Gln Asp Tyr(SO3) Thr Gly Trp Phe Asp Phe–NH2], and caerulein 2.1 [pGlu Gln Asp Tyr(SO3) Thr Gly Ala His Met Phe–NH2], all of which are smooth muscle active. The major peptide, citropin 1.2 [Gly Leu Phe Asp Ile Ile Lys Lys Val Ala Ser Val Val Gly Gly Leu–NH2], is a wide-spectrum antibiotic and anticancer agent at the micromolar concentration. Citropin 1.2 also inhibits the formation of nitric oxide by the enzyme neuronal nitric oxide synthase (nNOS) at the micromolar concentration. Another peptide, citropin 2.2 [Gly Leu Ile Ser Ile Gly Lys Ala Leu Gly Gly Leu Ile Val Asp Val Leu Lys Pro Lys Ser–OH], also inhibits nNOS.
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8

Yong-Cun, Yang, Chi Shao-Ming, Liu Ming-Hua, Huang Rong, Wang Yu-Fei, Jing Bi, and Zhao Yan. "Spectrophotometric study of the selective binding behavior of aliphatic oligopeptides by bridged bis(β-cyclodextrin) linked by a 4,4′-diaminodiphenyl disulfide tether." Canadian Journal of Chemistry 88, no. 12 (December 2010): 1205–12. http://dx.doi.org/10.1139/v10-148.

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The conformation and binding behavior of 4,4′-diaminodiphenyl disulfide bridged bis(β-cyclodextrin) (1) towards representative aliphatic oligopeptides, i.e., Leu-Gly, Gly-Leu, Glu-Glu, Met-Met, Gly-Gly, Gly-Gly-Gly, and Gly-Pro, were investigated by circular dichroism, fluorescence, and 1H and 2D NMR spectroscopy at 25 °C in phosphate buffer (pH 7.20). The results indicated that 1 acts as an efficient fluorescent sensor and displays remarkable fluorescence enhancement upon addition of optically inert oligopeptides. Owing to the cooperative host–linker–guest binding mode in which the linker and guest are coincluded in the two cyclodextrin cavities, the bis(β-cyclodextrin) 1 gives high binding constants of up to 103–104 (mol/L)–1 for oligopeptides. The bis(β-cyclodextrin) 1 can recognize not only the size and shape of oligopeptides but also the hydrophobicity, giving an exciting residue selectivity of up to 61.3 for the Gly-Leu/Glu-Glu pair. These phenomena are discussed from the viewpoints of multiple recognition and induce-fit interactions between host and guest.
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9

Zhang, Jing-Bo, Yu-Qin Zhao, Yu-Mei Wang, Chang-Feng Chi, and Bin Wang. "Eight Collagen Peptides from Hydrolysate Fraction of Spanish Mackerel Skins: Isolation, Identification, and In Vitro Antioxidant Activity Evaluation." Marine Drugs 17, no. 4 (April 13, 2019): 224. http://dx.doi.org/10.3390/md17040224.

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A previous report indicated that collagen hydrolysate fraction (F7) from Spanish mackerel (Scomberomorous niphonius) skins showed high reducing power and radical scavenging activities on 2,2-Diphenyl-1-picrylhydrazyl (DPPH) (EC50 value of 1.57 mg/mL) and hydroxyl (EC50 value of 1.20 mg/mL). In this work, eight peptides were isolated from F7 and identified as Gly-Pro-Tyr (GPY, 335.31 Da), Gly-Pro-Thr-Gly-Glu (GPTGE, 459.47 Da), Pro-Phe-Gly-Pro-Asp (PFGPD, 531.52 Da), Gly-Pro-Thr-Gly-Ala-Lys (GPTGAKG, 586.65 Da), Pro-Tyr-Gly-Ala-Lys-Gly (PYGAKG, 591.69 Da), Gly-Ala-Thr-Gly-Pro-Gln-Gly (GATGPQG, 586.61 Da), Gly-Pro-Phe-Gly-Pro-Met (GPFGPM, 604.73 Da), and Tyr-Gly-Pro-Met (YGPM, 466.50 Da), respectively. Among them, PFGPD, PYGAKG, and YGPM exhibited strong radical scavenging activities on DPPH (EC50 values of 0.80, 3.02, and 0.72 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), hydroxyl (EC50 values of 0.81, 0.66, and 0.88 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), superoxide anion (EC50 values of 0.91, 0.80, and 0.73 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) cation (EC50 values of 0.86, 1.07, and 0.82 mg/mL for PFGPD, PYGAKG, and YGPM, respectively) in a positive concentration–activity relationship. Furthermore, PFGPD, PYGAKG, and YGPM could effectively reduce Fe3+ to Fe2+ and inhibit lipid peroxidation. Hence, eight collagen peptides from hydrolysate of Spanish mackerel skins might be served as antioxidant candidates for various industrial applications.
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10

Attia, Youssef A., Fulvia Bovera, Jinquan Wang, Mohammed A. Al-Harthi, and Woo Kyun Kim. "Multiple Amino Acid Supplementations to Low-Protein Diets: Effect on Performance, Carcass Yield, Meat Quality and Nitrogen Excretion of Finishing Broilers under Hot Climate Conditions." Animals 10, no. 6 (June 3, 2020): 973. http://dx.doi.org/10.3390/ani10060973.

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The objective of this study was to evaluate the effect of low-protein diets with amino acid supplementation on growth performance, carcass yield, meat quality and nitrogen excretion of broilers raised under hot climate conditions during the finisher period. In trial 1, broilers from 28 to 49 days of age were fed 18% crude protein (CP) as a positive control or 15% CP supplemented with (1) DL-methionine (Met) + L-lysine (Lys), (2) Met + Lys + L-Arginine (Arg), or (3) Met + Lys + L-Valine (Val). In trial 2, broilers from 30 to 45 days of age, were fed an 18% CP diet as a positive control or 15% CP supplemented with Met, Lys, Arg, Val, L-Isoleucine (Ile) or combination with glycine (Gly) and/or urea as nitrogen sources: (1) Met + Lys, (2) Met + Lys + Arg, (3) Met + Lys + Val, (4) Met + Lys + Ile, (5) Met + Lys + Arg +Val + Ile + Gly, and (6) Met+ Lys + Arg + Val + Ile + Gly + urea. Protein use was improved by feeding low-protein amino acid-supplemented diets as compared to the high-protein diet. Feeding 15% crude protein diet supplemented with only methionine and lysine had no negative effects on carcass yield, CP, total lipids and moisture% of breast meat while decreasing nitrogen excretion by 21%.
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11

Podstawka, Edyta, Yukihiro Ozaki, and Leonard M. Proniewicz. "Part III: Surface-Enhanced Raman Scattering of Amino Acids and Their Homodipeptide Monolayers Deposited onto Colloidal Gold Surface." Applied Spectroscopy 59, no. 12 (December 2005): 1516–26. http://dx.doi.org/10.1366/000370205775142520.

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Surface-enhanced Raman scattering (SERS) spectra were measured for monolayers of various amino acids: L-methionine (Met), L-cysteine (Cys), L-glycine (Gly), L-leucine (Leu), L-phenylalanine (Phe), and L-proline (Pro) and their homodipeptides (Met-Met, Cys-Cys, Gly-Gly, Leu-Leu, Phe-Phe, and Pro-Pro) deposited onto a colloidal gold surface. Orientation of amino acids and their homodipeptides, as well as specific-competitive interactions of their functional groups with the gold surface, were predicted by detailed spectral analysis of the obtained SERS spectra. The analysis performed allowed us to propose a particular surface geometry for each amino acid and homodipeptide on the gold surface. In addition, we compared the structures of these molecules adsorbed on colloidal gold and silver surfaces.
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12

Djuran, Milo I., and Snezana U. Milinkovic´. "1H N.M.R. investigations of the selective intramolecular migration of a platinum(II) complex from methionine sulfur to imidazole N 1 in N-acetylated L-methionyl-L-histidine." Australian Journal of Chemistry 53, no. 8 (2000): 645. http://dx.doi.org/10.1071/ch00065.

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Reactions of two platinum(II) complexes [Pt(dien)Cl]+ and [Pt(Gly-Met-S,N,N´)Cl], in which dien is diethylenetriamine and Gly-Met is the dipeptide glycyl-L-methionine coordinated through the sulfur and two nitrogen atoms, with N-acetylated dipeptide L-methionyl-L-histidine (MeCO-Met-His) have been studied by 1H n.m.r. spectroscopy. All reactions were carried out in 50 mM phosphate buffer at pD 7.4 and at room temperature. In the initial stages of the reactions both platinum(II) complexes form a kinetically favoured platinum–peptide complex with unidentate coordination of MeCO-Met-His through the sulfur atom of the methionine residue. In the second stages of the reaction an intramolecular migration of a [Pt(dien)]2+ unit from the sulfur to the nitrogen atom of imidazole has been observed. This migration reaction is very slow and strongly selective to the N 1 atom of the imidazole ring of the histidine side chain. No migration of the platinum(II) complex was observed in the reaction between [Pt(Gly-Met-S,N,N´)Cl] and the dipeptide MeCO-Met-His. It was found that the latter complex, with a more sterically hindered Gly-Met ligand, reacts more slowly with thioether-containing molecules than [Pt(dien)Cl]+ and forms a more stable platinum–sulfur bond. This study is an important step in the development of new platinum(II) complexes for selective covalent modification of peptides and proteins.
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13

ARKIN, HANDAN, and TARIK ÇELİK. "STRUCTURE OF ENERGY LANDSCAPE OF SHORT PEPTIDES." International Journal of Modern Physics C 14, no. 01 (January 2003): 113–20. http://dx.doi.org/10.1142/s0129183103004267.

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We have simulated, as a showcase, the pentapeptide Met-enkephalin (Tyr-Gly-Gly-Phe-Met) to visualize the energy landscape and to investigate the conformational coverage by the multicanonical method. We obtained a three-dimensional topographic picture of the whole energy landscape by plotting the histogram with respect to energy (temperature) and the order parameter, which gives the degree of resemblance of any created conformation with the global energy minimum.
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14

Ivanova, B. B., M. G. Arnaudov, St Todorov, W. S. Sheldrick, and H. Mayer-Figge. "Structural analysis of the tripeptide glycyle-methionyl-glycine (H-Gly-Met-Gly-OH) and its hydrochloride." Structural Chemistry 17, no. 1 (February 2006): 49–56. http://dx.doi.org/10.1007/s11224-006-9034-0.

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15

Kasafírek, Evžen, Ladislav Fukal, and Jan Káš. "Chromogenic substrates for papain with a C-terminal S-benzylcysteine residue." Collection of Czechoslovak Chemical Communications 53, no. 12 (1988): 3197–205. http://dx.doi.org/10.1135/cccc19883197.

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Two types of chromogenic substrates for papain were prepared, namely p-nitroanilides of N-acetyltripeptides of general formula Ac-Leu-Leu-A-NAn, where A = Gly, Ala, Leu, and p-nitroanilides of 3-carboxypropionyldi- and tripeptides of general formula Suc-B-Cys(Bzl)-NAn, where B = Gly, Gly-Gly, Ala, Ala-Ala, Leu, Leu-Leu, Gly-Leu, Leu-Ala and Ala-Met. The values of Km, kcat and C (kcat/Km) for these substrates were determined. Suc-Leu-Leu-Cys(Bzl)-NAn is the best substrate for papain its C being 60 000 mol-1 l s-1.
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16

Rajković, Snežana, Beata Warżajtis, Marija D. Živković, Biljana Đ. Glišić, Urszula Rychlewska, and Miloš I. Djuran. "Hydrolysis of Methionine- and Histidine-Containing Peptides Promoted by Dinuclear Platinum(II) Complexes with Benzodiazines as Bridging Ligands: Influence of Ligand Structure on the Catalytic Ability of Platinum(II) Complexes." Bioinorganic Chemistry and Applications 2018 (2018): 1–12. http://dx.doi.org/10.1155/2018/3294948.

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Dinuclear platinum(II) complexes, [{Pt(en)Cl}2(μ-qx)]Cl2·2H2O (1), [{Pt(en)Cl}2(μ-qz)](ClO4)2(2), and [{Pt(en)Cl}2(μ-phtz)]Cl2·4H2O (3), were synthesized and characterized by different spectroscopic techniques. The crystal structure of1was determined by single-crystal X-ray diffraction analysis, while the DFT M06-2X method was applied in order to optimize the structures of1–3. The chlorido Pt(II) complexes1–3were converted into the corresponding aqua species1a–3a, and their reactions with an equimolar amount of Ac–L–Met–Gly and Ac–L–His–Gly dipeptides were studied by1H NMR spectroscopy in the pH range 2.0 < pH < 2.5 at 37°C. It was found that, in all investigated reactions with the Ac–L–Met–Gly dipeptide, the cleavage of the Met–Gly amide bond had occurred, but complexes2aand3ashowed lower catalytic activity than1a. However, in the reactions with Ac–L–His–Gly dipeptide, the hydrolysis of the amide bond involving the carboxylic group of histidine was observed only with complex1a. The observed disparity in the catalytic activity of these complexes is thought to be due to different relative positioning of nitrogen atoms in the bridging qx, qz, and phtz ligands and consequent variation in the intramolecular separation of the two platinum(II) metal centers.
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17

Sratthaphut, Lawan, and Kanong Ruttanakorn. "Chemometrics-Assisted UV Spectrophotometric Method for Determination of Metformin Hydrochloride and Glyburide in Pharmaceutical Tablets." Advanced Materials Research 1060 (December 2014): 164–67. http://dx.doi.org/10.4028/www.scientific.net/amr.1060.164.

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This study aims to estimate simultaneously metformin hydrochloride (MET) and glyburide (GLY) in a multicomponent tablets dosage form by spectrophotometric method using chemometric approaches such as principal component regression (PCR) and partial least-squares regression (PLS). Because of highly overlapped in UV spectra and difference proportions of two active ingredients, the conventional univariate calibration methods was not allowed without previous separation. The linearity ranges used to construct the calibration matrix were selected in the ranges from 40.00 to 200.00 mg L-1for MET and from 1.00 to 10.00 mg L-1for GLY. The absorbances were measured in the wavelength range of 200-400 nm, using ethanol as solvent. The resulting UV spectra were subjected to PCR and PLS algorithms and the optimum numbers of principal components (PCs) were selected according to prediction residual error sum of squares (PRESS) values of leave-one out cross-validation. The number of PCs for MET and GLY were found to be 5, 3 by PCR and 5, 3 by PLS, respectively. A set of synthetic mixtures was employed to verify the models and the performance of the models were shown in the values of the root mean square error in prediction (RMSEP). RMSEP values of MET and GLY were 1.806, 0.256 for PCR and 1.802, 0.185 for PLS, respectively. The suitable calibration models were applied to the analysis of these compounds in pharmaceutical formulation.
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18

Uglem, Gary L., and Mark C. Lewis. "Specificity of the surface aminopeptidase in Moniliformis moniliformis (Acanthocephala)." Journal of Helminthology 60, no. 4 (December 1986): 288–92. http://dx.doi.org/10.1017/s0022149x00008506.

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ABSTRACTThe hydrolysis of various oligopeptides in solution by intact Moniliformis moniliformis was examined using paper chromatographic analysis of the incubation medium. In the presence of transport inhibitors, the respective peptide sub-units and/or amino acid residues accumulated in the bathing medium. Only peptides with serine, methionine, leucine or alanine at the NH2-terminal end of the peptide were hydrolysed. There was no hydrolysis when these amino acids were located internally or at the COOH-terminus indicating genuine aminopeptidase activity of the class, α-aminoacylpeptide hydrolase. Hydrolysis was negligible when the NH2-terminus was arginie, aspartic acid, glutamic acid, glutamic acid, glycine, histidine, lysine, phenylalanine, proline, tryptophan, tyrosine, or valine. In separate experiments, mediated uptake of 0.1 mM3H-leucine by the worms in 2 min was inhibited 100% by 5 mM unlabelled leucine or tri-serine, but only partially inhibited by 5 mM Ser-Gly (66%), 10 mM Ser-Gly (74%), 5 mM Leu-Leu (69%), 10 mM Leu-Leu (70%), 5 mM Leu-Gly (58%) or 5nM Met-Met (69%). Bacause the inhibitions produced by 5 mM Leu-Leu plus 5 mM Met-Met (79%) or 5 mM Leu-Leu plus 5 mM Ser-Gly (76%) were not additive, a single enzyme is indicated. The name serine aminopeptidase is proposed because of its preference for serine.
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19

Vasic, Ivana, and Marija D. Zivkovic. "Reactions of Platinum II Complexes with Sulfur- and Nitrogen-Containing Biomolecules: Selective Intermolecular Migration of the Thioether-Bound Platinum II Complex to the N7 Nitrogen Atom of Guanosine-5’-Monophosphate." Serbian Journal of Experimental and Clinical Research 19, no. 4 (December 1, 2018): 325–30. http://dx.doi.org/10.1515/sjecr-2017-0015.

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Abstract The interactions of platinum(II) complexes with nitrogen- and sulfur-containing biomolecules are responsible for aider antitumor activity due to attack on DNA or a variety of toxic side effects. Therefore, the monofunctional Pt(II) complexes, [Pt(Gly-Gly-N,N,O)I]+ (Gly-Gly is the dipeptide glycyl-glycine coordinated through the oxygen and two nitrogen atoms) and [Pt(Gly-L-Met-S,N,N)Cl] (Gly-L-Met is the dipeptide glycyl-L-methionine coordinated through the sulfur and two nitrogen atoms) have been used to study their interactions with S-methylglutathione (GS-Me) and guanosine- 5’-monophosphate (5’-GMP). All reactions have been studied by 1H NMR spectroscopy and at room temperature in 50 mM phosphate buffer at pD 7.4. The investigation of the competitive binding of 5’-GMP and GS-Me to the Pt(II) complexes (1:1:1 molar ratio) has shown that in the initial stages of the reaction the corresponding Pt(II) complex only reacts with GS-Me, and second step of the reaction is very slow intermolecular displacement of the S-bound thioether ligand with N7 atom of the guanine base of 5’-GMP. The obtained results have been analyzed in relation to the antitumor activity and toxicity of Pt(II) complexes.
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20

Kluh, Ivan, Ladislav Morávek, and Manfred Pavlík. "Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin." Collection of Czechoslovak Chemical Communications 54, no. 3 (1989): 803–10. http://dx.doi.org/10.1135/cccc19890803.

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Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.
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21

Zhang, Lun, Guo-Xu Zhao, Yu-Qin Zhao, Yi-Ting Qiu, Chang-Feng Chi, and Bin Wang. "Identification and Active Evaluation of Antioxidant Peptides from Protein Hydrolysates of Skipjack Tuna (Katsuwonus pelamis) Head." Antioxidants 8, no. 8 (August 19, 2019): 318. http://dx.doi.org/10.3390/antiox8080318.

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For the full use of fish by-products to produce antioxidant peptides, skipjack tuna (Katsuwonus pelamis) heads generated during can processing were defatted and hydrolyzed using the in vitro gastrointestinal (GI) digestion (pepsin–trypsin system) method and six antioxidant peptides (P1 to P6) were purified from the head hydrolysate (KPH) using ultrafiltration and serial chromatography methods. Six isolated peptides (P1 to P6) were identified as Val-Glu-Glu (VEE, P1), Trp-Met-Phe-Asp-Trp (WMFDW, P2), Asp-Ala-Gly-Pro-Tyr-Gly-Pro-Ile (DAGPYGPI, P3), Trp-Met-Gly-Pro-Tyr (WMGPY, P4), Glu-Arg-Gly-Pro-Leu-Gly-Pro-His (ERGPLGPH, P5), and Glu-Met- Gly-Pro-Ala (EMGPA, P6), respectively, using a protein sequencer and electrospray ionization-mass spectrometer. Among skipjack tuna head hydrolysates, fractions, and six isolated peptides (P1 to P6), WMFDW (P2), WMGPY (P4), and EMGPA (P6) showed the highest radical scavenging activities on 2,2-diphenyl-1-picrylhydrazyl (DPPH) (EC50 values of 0.31, 0.33, and 0.46 mg/mL for WMFDW, WMGPY, and EMGPA, respectively), hydroxyl (EC50 values of 0.30, 0.43, and 0.52 mg/mL for WMFDW, WMGPY, and EMGPA, respectively), and superoxide anion (EC50 values of 0.56, 0.38, and 0.71 mg/mL for WMFDW, WMGPY, and EMGPA, respectively). Moreover, WMFDW, WMGPY, and EMGPA showed strong capability in reducing power and lipd peroxidation inhibition in the linoleic acid system. In addition, WMFDW, WMGPY, and EMGPA can retain strong antioxidant activity at temperatures lower than 60 °C and pH values ranged from 5 to 9. The results showed that six isolated peptides (P1 to P6) from skipjack tuna heads, especially WMFDW, WMGPY, and EMGPA, might be applied in health care products acting as powerful antioxidant agents.
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22

Jha, Bhavya, Rajan Vyas, Jaya Bhushan, Devinder Sehgal, and Bichitra Kumar Biswal. "Structural insights into the substrate specificity of SP_0149, the substrate-binding protein of a methionine ABC transporter from Streptococcus pneumoniae." Acta Crystallographica Section F Structural Biology Communications 75, no. 7 (July 1, 2019): 520–28. http://dx.doi.org/10.1107/s2053230x19009038.

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Successful pathogenesis is a cumulative effect of the virulence factors of a pathogen and its capability to efficiently utilize the available nutrients from the host. Streptococcus pneumoniae, a Gram-positive opportunistic pathogen, may either reside asymptomatically as a nasopharyngeal commensal inside the human host or cause lethal diseases, including pneumonia, meningitis and sepsis. S. pneumoniae is known to acquire methionine (Met) from its host through a Met importer. Here, the crystal structure of the substrate-binding protein (SBP; SP_0149) of an ABC importer with Met bound is reported at a resolution of 1.95 Å. The three-dimensional structure of SBP shows that it is composed of two distinct domains, each consisting of a mixed β-sheet flanked by helices. The substrate, Met, is bound in the central part of the interface between the two domains. The overall structure of SP_0149 resembles those of SBPs from other reported bacterial Met and Gly-Met dipeptide transporters. However, a detailed analysis of these structures shows notable variations in the amino-acid composition of the substrate-binding pockets of the SP_0149–Met and GmpC–Gly-Met structures. In particular, SP_0149 harbors Thr212 and Tyr114, whereas the corresponding residues in GmpC are Gly and Val. This difference is likely to be the underlying basis for their differential substrate specificity. In summary, the structure of the SP_0149–Met complex provides insights into the transport function of SP_0149 and its interactions with methionine. It opens up avenues for the rational design of inhibitors of SP_0149 through a structure-mediated approach.
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23

Matsumoto, M., J. Park, K. Sugano, and T. Yamada. "Biological activity of progastrin posttranslational processing intermediates." American Journal of Physiology-Gastrointestinal and Liver Physiology 252, no. 3 (March 1, 1987): G315—G319. http://dx.doi.org/10.1152/ajpgi.1987.252.3.g315.

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We recently identified carboxyl-terminally extended progastrin posttranslational processing intermediates in G cells of the gastric antrum and demonstrated that they are cosecreted with gastrin. To determine the physiological significance of these intermediates, we examined the biological activity of two synthetic gastrin precursor analogues that correspond to hexagastrin with carboxyl-terminal extensions, Tyr-Gly-Trp-Met-Asp-Phe-Gly (GL-7) and Tyr-Gly-Trp-Met-Asp-Phe-Gly-Arg-Arg (GL-9) on gastric parietal and D cells isolated from canine fundic mucosa. Both analogues were as efficacious as gastrin heptadecapeptide in displacing 125I-[Leu15]gastrin from binding sites on the two cell types and in stimulating [14C]aminopyrine uptake by parietal cells and somatostatin release from D cells. However, both analogues were 10(4)- to 10(5)-fold less potent than gastrin heptadecapeptide in these activities. Our results indicate that progastrin processing intermediates do not have physiologically relevant actions under normal circumstances and support the notion that carboxyl-terminally amidated peptides such as gastrin require the amide moiety for biological activity.
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Wu, Dan, Xiaomeng Xu, Na Sun, Dongmei Li, Beiwei Zhu, and Songyi Lin. "AGLPM and QMDDQ peptides exert a synergistic action on memory improvement against scopolamine-induced amnesiac mice." Food & Function 11, no. 12 (2020): 10925–35. http://dx.doi.org/10.1039/d0fo02570d.

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This study aimed to explore the synergistic action of pentapeptides Gln-Met-Asp-Asp-Gln (QMDDQ) and Ala-Gly-Leu-Pro-Met (AGLPM) on memory improvement against scopolamine-induced impairment in mice compared to those of either of the peptides alone.
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25

Lemay, François, Chakib Ameziane Hassani, and André G. Michel. "Structural requirements for molecular recognition by the Neurokinin receptors." Canadian Journal of Chemistry 68, no. 7 (July 1, 1990): 1186–91. http://dx.doi.org/10.1139/v90-183.

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Populations of lower energy conformers have been generated by conformational energy calculations, using empirical energy functions, for the C-terminal pentapeptide of Substance P (CH3-CO-Phe-Phe-Gly-Leu-Met-NH2), Neurokinins A and B (CH3-CO-Phe-Val-Gly-Leu-Met-NH2), and Eledoisin (CH3-CO-Phe-Ile-Gly-Leu-Met-NH2). The C-terminal sequences are greatly conserved in the Neurokinin and Tachychinin families of peptides and are mainly responsible for the molecular recognition. These sequences differ in the nature of the second residue. This substitution interferes with the recognition processes and modulates the specificities. A procedure based on a random generation of conformers, followed by energy minimizations, has been applied to produce the populations of conformers for the three pentapeptides. The conformational properties of the lower energy conformers have been analysed and compared with respect to the substitution of the second residue. Earlier nuclear magnetic resonance data as well as structure–activity relationship results have been interpreted in light of the proposed stable conformers. It is shown that the selectivity towards the NK3 receptor requires a structure with a restrained flexibility introduced at the second N-terminal residue. The selectivity towards the NK1 receptor is shown to be related to the presence of a constrained structure at the Gly residue. These structures suggest further chemical modifications be introduced in order to produce more selective and stable analogues. Keywords: peptide conformation, empirical energy, Neurokinin, molecular recognition.
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26

Woitzik, Daniela, Jürgen Weckesser, Roland Benz, Stefan Stevanovic, Günther Jung, and Jürg P. Rosenbusch. "Porin of Rhodobacter capsulatus: Biochemical and Functional Characterization." Zeitschrift für Naturforschung C 45, no. 6 (June 1, 1990): 576–82. http://dx.doi.org/10.1515/znc-1990-0602.

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Abstract The major outer membrane protein of Rhodobacter capsulatus 37 b4 (capsule-free) was iso­lated. Strong porin-activity was observed after reconstitution into artificial lipid bilayer mem­branes with a single channel conductance of 3.15 nS in Im KC1. The porin migrated as a broad, single band (Mr above 90,000) on sodium dodecyl sulfate polyacrylamide gel electro­ phoresis and dissociated into a single species of polypeptides (Mr 36,000) on treatment with EDTA (10 mM at 30 °C, 20 min) or by heating (100 °C, 5 min). Analytical ultracentrifugation studies demonstrated the native porin to be a trimer. The monomers chromatofocused as a single, sharp peak on fast performance liquid chromatography and only one band, corre­ sponding to an isoelectric point of about 4.0, was obtained on isoelectric focusing. Gas-phase sequencing of the 23 N-terminal residues revealed Glu-Val-Lys-Leu-Ser-Gly-Asp-Ala-Arg-Met-Gly-Val-Met-Tyr-Asn-Gly-Asp-Asp-X-Asn-Phe-Ser-Ser.
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27

SHIMOSEGAWA, Tooru, Masaru KOIZUMI, Takayoshi TOYOTA, Yoshio GOTO, Tooru MOCHIZUKI, Chizuko YANAIHARA, and Noboru YANAIHARA. "Met-Enkephalin-Arg-Gly-Leu-Like Immunoreactivity-Containing Nerve Elements in the Guinea-Pig Intestine." Folia Endocrinologica Japonica 61, no. 8 (1985): 802–15. http://dx.doi.org/10.1507/endocrine1927.61.8_802.

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28

Houdi, Abdulghani A., Krystyna Pierzchala, Lesley Marson, Miklos Palkovits, and Glen R. Van Loon. "Nicotine-induced alteration in Tyr-Gly-Gly and Met-enkephalin in discrete brain nuclei reflects altered enkephalin neuron activity." Peptides 12, no. 1 (January 1991): 161–66. http://dx.doi.org/10.1016/0196-9781(91)90183-p.

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29

Bradford, AM, MJ Raftery, JH Bowie, MJ Tyler, JC Wallace, GW Adams, and C. Severini. "Novel Uperin Peptides From the Dorsal Glands of the Australian Floodplain Toadlet Uperoleia inundata." Australian Journal of Chemistry 49, no. 4 (1996): 475. http://dx.doi.org/10.1071/ch9960475.

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The dorsal glandular extract of the floodplain toadlet Uperoleia inundata contains more than 50 peptides: we report the amino acid sequences and bioactivity data of 13 of these. The peptides have been sequenced by using a combination of mass spectrometry and automated Edman sequencing. Ten of the peptides have been synthesized in order to confirm their structures, and to enable bioassays to be carried out. Ten peptides are host- defence agents, including ( i ) a powerful new neuropeptide of the tachykinin family which we name uperin 1.1 [ pGlu Ala Asp Pro Asn Ala Phe Tyr Gly Leu Met (NH2)], and (ii) nine antibiotic peptides including five uperins 2 [e.g. uperin 2.1, Gly Ile Val Asp Phe Ala Lys Lys Val Val Gly Gly Ile Arg Asn Ala Leu Gly Ile (OH)], three uperins 3 [e.g. uperin 3.1, Gly Val Leu Asp Ala Phe Arg Lys Ile Ala Thr Val Val Lys Asn Val Val (NH2)] and uperin 4.1 [ Gly Val Gly Ser Phe Ile His Lys Val Val Ser Ala Ile Lys Asn Val Ala (NH2)]. The function of the three other characterized peptides in the amphibian integument is not known, viz. ( i ) uperin 5.1 [ Phe Gln Phe Val Asn Pro Ser Asp Ile Val Phe Gly Ser (OH)] and (ii) the two uperins 6 [e.g. uperin 6.1, Gly Leu Ala Gly Ala Ile Ser Ser Ala Leu Asp Lys Leu Lys Gln Ser Gln Leu Ile Lys Asn Tyr Ala Lys Lys Leu Gly Tyr Pro Arg (OH)].
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30

Nimmo, H. G., F. Douglas, C. Kleanthous, D. G. Campbell, and C. MacKintosh. "Identification of a cysteine residue at the active site of Escherichia coli isocitrate lyase." Biochemical Journal 261, no. 2 (July 15, 1989): 431–35. http://dx.doi.org/10.1042/bj2610431.

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Escherichia coli isocitrate lyase was inactivated by iodacetate in a pseudo-first-order process. Complete inactivation was associated with the incorporation of only one carboxymethyl group per enzyme subunit. The substrate and products of the enzyme protected against inactivation, suggesting that the reactive group may be located at the active site. Isolation and sequencing of a carboxymethylated peptide showed that the modified residue was a cysteine, in the sequence Cys-Gly-His-Met-Gly-Gly-Lys. The reactivity of isocitrate lyase to iodoacetate declined with pH, following a titration curve for a group of pKa 7.1. The Km of the enzyme for isocritrate declined over the same pH range.
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31

Li, Xiaofei, Lingyan Zhang, Liyang Zhang, Lin Lu, and Xugang Luo. "Effect of iron source on iron absorption by in situ ligated intestinal loops of broilers." Animal Production Science 57, no. 2 (2017): 308. http://dx.doi.org/10.1071/an15531.

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Two experiments were conducted to investigate the effect of iron (Fe) source on Fe absorption by in situ ligated intestinal loops of broilers. In Experiment 1, in situ ligated intestinal loops from Fe-deficient chicks (29 days old) were perfused with solutions containing 0.45 mmol Fe/L from FeSO4 (FeSO4·7H2O), Fe-Gly chelate, Fe-Met chelate, one of three Fe-amino acid or protein complexes with weak, moderate or extremely strong complex strength (Fe-Met W, Fe-Pro M, or Fe-Pro ES), or the mixtures of FeSO4 with either Gly or Met (Fe + Gly or Fe + Met), respectively, up to 30 min. In Experiment 2, in situ ligated duodenal loops from Fe-deficient chicks (29 days old) were perfused with solutions containing 0–3.58 mmol Fe/L from FeSO4, Fe-Met W, Fe-Pro M, or Fe-Pro ES up to 30 min. The absorptions of Fe from both inorganic and organic Fe sources in the ligated duodenum were ~1.35–2.8 times higher (P < 0.05) than that in the ligated jejunum or ileum. The absorption of Fe as Fe-Pro M or Fe-Pro ES was higher (P < 0.05) than that of Fe as inorganic Fe or Fe-Met W at Fe concentration of 3.58 mmol/L. The absorption kinetics of Fe from organic and inorganic Fe sources in the ligated duodenal loops followed a saturable process as determined by regression analysis of concentration-dependent absorption rates. The maximum absorption rate and Michaelis–Menten constant values in the ligated duodenal loops were higher (P < 0.05) for Fe-Pro M and Fe-Pro ES than for FeSO4 and Fe-Met W. The results from this study indicate that the duodenum was the main site of Fe absorption in the intestines of broilers; organic Fe sources with stronger complex strength values showed higher Fe absorptions at a higher concentration of added Fe; and the simple mixture of FeSO4 with amino acids did not increase Fe absorption.
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32

Funata, N., M. Fukayama, K. Sugano, and M. Koike. "Intracellular topography of glycine-extended pro-gastrin-processing intermediates in human antral mucosa: an electron-microscopic immunocytochemical study." Journal of Histochemistry & Cytochemistry 37, no. 3 (March 1989): 287–92. http://dx.doi.org/10.1177/37.3.2918220.

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To identify and characterize the subcellular topography of glycine-extended pro-gastrin-processing intermediates (G-Gly) in human antral mucosa, we performed an electron microscopic immunocytochemical study using region-specific antisera generated against the synthetic peptide, Tyr-Gly-Trp-Met-Asp-Phe-Gly (GL7), and C-terminal-specific anti-gastrin antisera. As has been previously reported, G-cells contained both electron-dense and electron-lucent granules, with a range of intermediate forms. Gastrin immunoreactivity was demonstrated in almost all granules of each type, whereas anti-GL7 antisera immunostained chiefly electron-dense granules. The relative ratio of GL7/gastrin granules varied among different cells but was approximately 1:10 on average. Other cytoplasmic organelles were devoid of specific labeling for GL7 or gastrin. As we have assumed that G-Gly serves as the immediate precursor for each molecular form of gastrin, electron-dense granules with high labeling for GL7 are regarded as the principal site for conversion of G-Gly to gastrin. This speculation supports many previous reports that electron-dense granules are immature and that the granules become less electron-dense with maturation.
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33

Suzuki, Takeo, Kenjyo Miyauchi, Tsutomu Suzuki, Shin-ichi Yokobori, Naoki Shigi, Akiko Kondow, Nono Takeuchi, Akihiko Yamagishi, and Kimitsuna Watanabe. "Taurine-containing Uridine Modifications in tRNA Anticodons Are Required to Decipher Non-universal Genetic Codes in Ascidian Mitochondria." Journal of Biological Chemistry 286, no. 41 (August 26, 2011): 35494–98. http://dx.doi.org/10.1074/jbc.m111.279810.

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Variations in the genetic code are found frequently in mitochondrial decoding systems. Four non-universal genetic codes are employed in ascidian mitochondria: AUA for Met, UGA for Trp, and AGA/AGG(AGR) for Gly. To clarify the decoding mechanism for the non-universal genetic codes, we isolated and analyzed mitochondrial tRNAs for Trp, Met, and Gly from an ascidian, Halocynthia roretzi. Mass spectrometric analysis identified 5-taurinomethyluridine (τm5U) at the anticodon wobble positions of tRNAMet(AUR), tRNATrp(UGR), and tRNAGly(AGR), suggesting that τm5U plays a critical role in the accurate deciphering of all four non-universal codes by preventing the misreading of pyrimidine-ending near-cognate codons (NNY) in their respective family boxes. Acquisition of the wobble modification appears to be a prerequisite for the genetic code alteration.
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34

Conlon, J. M., J. H. Youson, and J. Whittaker. "Structure and receptor-binding activity of insulin from a holostean fish, the bowfin (Amia calva)." Biochemical Journal 276, no. 1 (May 15, 1991): 261–64. http://dx.doi.org/10.1042/bj2760261.

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The holostean fishes are the extant representatives of the primitive ray-finned fishes from which the present-day teleosts may have evolved. The primary structure of insulin from a holostean fish, the bowfin (Amia calva), was established as: A-chain: Gly-Ile-Val-Glu-Gln-Cys-Cys-Leu-Lys-Pro-Cys-Thr-Ile-Tyr-Glu-Met-Glu- Lys-Tyr-Cys-Asn B-chain: Ala-Ala-Ser-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Phe-Leu- Val-Cys-Gly-Glu-Ser-Gly-Phe-Phe-Tyr-Asn-Pro-Asn-Lys-Ser This amino acid sequence contains several substitutions (methionine at A16, phenylalanine at B16 and serine at B22) at sites that have been strongly conserved in other vertebrate species and that may be expected to influence biological activity. Consistent with this prediction, bowfin insulin was approx. 14-fold less potent than pig insulin in inhibiting the binding of [125I-Tyr-A14](human insulin) to transfected mouse NIH 3T3 cells expressing the human insulin receptor.
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35

De Toni, C. H., M. F. Richter, J. R. Chagas, J. AP Henriques, and C. Termignoni. "Purification and characterization of an alkaline serine endopeptidase from a feather-degradingXanthomonas maltophiliastrain." Canadian Journal of Microbiology 48, no. 4 (April 1, 2002): 342–48. http://dx.doi.org/10.1139/w02-027.

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A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis. This enzyme has a molecular mass of 36 kDa, an optimum pH of 9.0, and an optimum temperature of 60°C. The inhibitory profile using protease inhibitors shows that this enzyme is a serine endopeptidase. Besides keratin, the enzyme is active upon the substrates azokeratin, azocasein, and the following fluorogenic peptide substrates: Abz-Leu-Gly-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Gln-EDDnp, Abz-Lys-Leu-Cys(SBzl)-Gly-Pro-Lys-Gln-EDDnp, and Abz-Lys-Pro-Cys(SBzl)-Phe-Ser-Lys-Gln-EDDnp.Key words: serine endopeptidase, Xanthomonas maltophilia, keratinase, alkaline endopeptidase.
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36

Abe, Jun, Hitoshi Okamura, Shigeru Makino, Noboru Yanaihara, and Yasuhika Ibata. "Immunocytochemical distribution of [Met]enkephalin-Arg-Gly-Leu immunoreactivity in the rat diencephalon." Brain Research Bulletin 19, no. 6 (December 1987): 735–41. http://dx.doi.org/10.1016/0361-9230(87)90061-x.

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37

Wang, Caihong, Fengqi Zhao, Jianxin Liu, and Hongyun Liu. "Dipeptide (Methionyl-Methionine) Transport and Its Effect on β-Casein Synthesis in Bovine Mammary Epithelial Cells." Cellular Physiology and Biochemistry 49, no. 2 (2018): 479–88. http://dx.doi.org/10.1159/000492987.

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Background/Aims: The aim of this study was to investigate the transport properties and utilization of methionyl-methionine dipeptide (Met-Met) in β-casein (β-CN) synthesis in bovine mammary epithelial cells (BMECs). Methods: The transport properties were studied for the effects of time, pH, concentration, temperature and inhibitors using Met-Met-FITC in BMECs. BMECs were treated with different concentrations of Met-Met (0, 20, 40, 80, 120 and 160 µg/ml). In several experiments, the cells were treated with Janus kinase 2 (JAK2) inhibitor (tyrphostin AG-490, 50 µM) and mammalian target of rapamycin (mTOR) inhibitor (rapamycin, 100 ng/ml). Results: The uptake of Met-Met-FITC by BMECs was rapid during the first fifteen minutes and became saturated after 15 minutes. The transport of Met-Met-FITC in BMECs exhibited a Michaelis constant of 52.4 µM and maximum transport velocity of 14.8 pmol/min/mg protein. The uptake of Met-Met-FITC in BMECs was pH-dependent, peaked at pH 6.5 and was significantly inhibited by other peptides, including Met-Lys, Lys-Lys, Gly-Met, Gly-Leu and Met-Leu. Knocking down the peptide transporter 2 (PepT2) with small interference RNA markedly decreased Met-Met-FITC uptake. Met-Met concentration-dependently increased the PepT2 expression and β-CN synthesis in BMECs with an optimal concentration of 80 µg/ml. At 80 µg/ml, Met-Met also enhanced the cell viability and cyclin D1 expression and promoted cell cycle transition from G1 phase to S phase. In addition, 80 µg/ml Met-Met increased the mRNA abundance of JAK2 and signal transducer and activator of transcription 5 (STAT5) and enhanced the phosphorylation of JAK2, STAT5, mTOR, p70 ribosomal S6 kinase 1 and eukaryotic initiation factor 4E binding protein 1. The inhibition of JAK2 and mTOR significantly decreased Met-Met-induced increase in cell viability and β-CN synthesis in BMECs. Conclusion: Our data elucidated the properties of peptide transporter and its effect on β-CN synthesis in BMECs. Met-Met, taken up by PepT2, enhances cell proliferation and promotes β-CN synthesis by activating JAK2-STAT5 and mTOR signaling pathways in BMECs.
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38

Md. Abdur Rauf, Shah, Per I. Arvidsson, Fernando Albericio, Thavendran Govender, Glenn E. M. Maguire, Hendrik G. Kruger, and Bahareh Honarparvar. "The effect of N-methylation of amino acids (Ac-X-OMe) on solubility and conformation: a DFT study." Organic & Biomolecular Chemistry 13, no. 39 (2015): 9993–10006. http://dx.doi.org/10.1039/c5ob01565k.

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N-Methylation of amino acid derivatives (Ac-X-OMe, X = Gly, Val, Leu, Ile, Phe, Met, Cys, Ser, Asp and His) leads to an increase in aqueous solubility, lipophilicity and lowering of the cis/trans amide conformational energy barrier (EA).
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Pai, Hyunjoo, Hoan-Jong Lee, Eun-Hwa Choi, Jungmin Kim, and George A. Jacoby. "Evolution of TEM-Related Extended-Spectrum β-Lactamases in Korea." Antimicrobial Agents and Chemotherapy 45, no. 12 (December 1, 2001): 3651–53. http://dx.doi.org/10.1128/aac.45.12.3651-3653.2001.

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ABSTRACT TEM-52, differing from TEM-1 by having the substitutions Glu-104→Lys, Met-182→Thr, and Gly-238→Ser, has previously been described as the most prevalent extended-spectrum β-lactamase (ESBL) in Korea. In a further survey, we discovered the ESBLs TEM-15, which is like TEM-52 but lacks the substitution at residue 182, and TEM-88, which is like TEM-52 with an additional Gly-196→Asp substitution. TEM-88 retained the activity of TEM-52 against moxalactam. Otherwise, the kinetic properties of the three ESBLs failed to show an advantage to this evolution.
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40

Hlaváček, Jan, Jana Pírková, Miroslava Žertová, Jan Pospíšek, Lenka Maletínská, and Jiřina Slaninová. "Cholecystokinin Heptapeptide Analogues with Multiple Modification in Peptide Chain." Collection of Czechoslovak Chemical Communications 58, no. 11 (1993): 2761–65. http://dx.doi.org/10.1135/cccc19932761.

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Using solid phase synthesis we prepared the cholecystokinin fragment Boc-CCK-7 (Boc-Tyr(SO3-Na+)-Met-Gly-Trp-Met-Asp-Phe-NH2) Ia and its seven analogues Ib - Ih. In the analogues Ib and Ic the Met residue in the carboxyterminal part of the molecule was substituted for L- or D-Phe Me3. In the analogues Id and Ie with Phe residue substituted by L- or D-Phe Me3 the Neo was inserted in the place of this Met residue and in the analogues If and Ig, an addition to PheMe3 substitution in the carboxyterminus, both Met residues were replaced for Neo. This dual substitution for Met residues was also applied in the analogue Ih with coded Phe residue in the C-terminus.
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41

Lau, HK. "Anticoagulant function of a 24-Kd fragment isolated from human fibrinogen A alpha chains." Blood 81, no. 12 (June 15, 1993): 3277–84. http://dx.doi.org/10.1182/blood.v81.12.3277.bloodjournal81123277.

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A fibrinogen fragment obtained by limited-plasmin proteolysis has been isolated and purified to apparent homogeneity by gel filtrations. This fragment, denoted as 24-Kd fragment, has an apparent M(r) approximately 24,000 and contains an N-terminal sequence of met-glu-leu-glu-arg-pro- gly-gly-asn-glu-ile. The fragment contains a large number of acidic amino acid residues, and its amino acid composition is similar to several fibrinogen A alpha chains degradation fragments isolated previously. It corresponds to a peptide of the fibrinogen A alpha chains, the N-terminal of which starts at alpha Met-240. This peptide delays thrombin plasma clotting time. It does not bind calcium ions and does not inhibit thrombin's amidolytic activity. It binds to immobilized fibrin but not fibrinogen. It also inhibits the polymerization of desAA and desAABB fibrin monomers by simultaneously decreasing the maximum rate and the maximum level of the polymerization reaction. However, the initial lag period of this reaction is not affected by the fragment.
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42

Qiu, Wang, Yang, Zhao, Chi, and Wang. "Gelatin and Antioxidant Peptides from Gelatin Hydrolysate of Skipjack Tuna (Katsuwonus pelamis) Scales: Preparation, Identification and Activity Evaluation." Marine Drugs 17, no. 10 (October 3, 2019): 565. http://dx.doi.org/10.3390/md17100565.

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For full use of fish by-products, scale gelatin (TG) and antioxidant peptides (APs) of skipjack tuna (Katsuwonus pelamis) were prepared, and their properties were characterized using an amino acid analyzer, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier transform infrared spectroscopy (FTIR), electrospray ionization mass spectrometers (ESI-MS), and radical scavenging assays. The results indicate that TG with a yield of 3.46 ± 0.27% contained Gly (327.9 ± 5.2 residues/1000 residues) as the major amino acid and its imino acid content was 196.1 residues/1000 residues. The structure of TG was more unstable than that of type I collagen from scales of skipjack tuna (TC) and TG was more suitable for preparation of hydrolysate by protease than mammalian gelatins. Therefore, TG was separately hydrolyzed under five proteases (pepsin, papain, trypsin, neutrase, and alcalase) and ten APs (TGP1–TGP10) were isolated from the alcalase-hydrolysate. Among them, TGP5, TGP7, and TGP9 with high antioxidant activity were identified as His-Gly-Pro-Hyp-Gly-Glu (TGP5), Asp-Gly-Pro-Lys-Gly-His (TGP7) and Met-Leu-Gly-Pro-Phe-Gly-Pro-Ser (TGP9), respectively. Furthermore, TGP5, TGP7, and TGP9 exhibited a high radical scavenging capability on 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (EC50 values of 1.34, 0.54, and 0.67 mg/mL, respectively), hydroxyl radical (EC50 values of 1.03, 0.41, and 0.74 mg/mL, respectively), and superoxide anion radical (EC50 values of 1.19, 0.71, and 1.59 mg/mL, respectively). These results suggest that three APs (TGP5, TGP7, and TGP9), especially TGP7, have a strong antioxidant activity and could act as potential antioxidant ingredients applied in functional products.
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Murugesan, Muthu, Murugapillai Venugopal, and Rajadas Jayakumar. "Aggregation of a tetrapeptide derivative [Boc-Ile-Gly-Met-Thr(Bzl)-OBzl] in chloroform." Journal of the Chemical Society, Perkin Transactions 2, no. 10 (1997): 1959–63. http://dx.doi.org/10.1039/a702359f.

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44

Kumari, Bandana, Ravindra Kumar, and Manish Kumar. "Identifying residues that determine palmitoylation using association rule mining." Bioinformatics 35, no. 17 (January 12, 2019): 2887–90. http://dx.doi.org/10.1093/bioinformatics/btz003.

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Abstract Motivation In eukaryotes, palmitoylation drives several essential cellular mechanisms like protein sorting, protein stability and protein–protein interaction. Several amino acids namely Cys, Gly, Ser, Thr and Lys undergo palmitoylation. But very little is known about the amino acid patterns that promote palmitoylation. Results We deduced presence of statistically significant amino acids around palmitoylation sites and their association with different palmitoylated residues i.e. Cys, Gly and Ser. The results suggest that palmitoylation, irrespective of its target residue, generally occurs at sites where Cys, Leu, Lys, Arg, Ser and Met are abundant. Furthermore, functional properties of the three types of palmitoylated proteins were compared. We observed similar functional behavior of Cys and Gly palmitoylated proteins but proteins with Ser palmitoylation showed distinctiveness from remaining two. Motif-wise functional conservation was also observed in Cys palmitoylated proteins. We also did functional annotation of predicted human palmitoylome. Supplementary information Supplementary data are available at Bioinformatics online.
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SHIMOSEGAWA, Tooru, Mizuo KOBARI, Makoto YAMBE, Masaru KOIZUMI, Takayoshi TOYOTA, Yoshio GOTO, Shigeru KOBAYASHI, Tooru MOCHIZUKI, Chizuko YANAIHARA, and Noboru YANAIHARA. "Met-Enkephalin-Arg-Gly-Leu-Like Immunoreactivity-Containing Nerve Fibers and Cell Bodies in the Abdominal Sympathetic Ganglia of the Rat." Folia Endocrinologica Japonica 61, no. 5 (1985): 581–91. http://dx.doi.org/10.1507/endocrine1927.61.5_581.

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46

Duve, H., A. H. Johnsen, A. G. Scott, and A. Thorpe. "Isolation, identification and functional significance of [Hyp2]Met-callatostatin and des Gly-Pro Met-callatostatin, two further post-translational modifications of the blowfly neuropeptide Met-callatostatin." Regulatory Peptides 57, no. 3 (June 1995): 237–45. http://dx.doi.org/10.1016/0167-0115(95)00037-c.

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47

Zhang, Shuang-Yi, Guo-Xu Zhao, Shi-Kun Suo, Yu-Mei Wang, Chang-Feng Chi, and Bin Wang. "Purification, Identification, Activity Evaluation, and Stability of Antioxidant Peptides from Alcalase Hydrolysate of Antarctic Krill (Euphausia superba) Proteins." Marine Drugs 19, no. 6 (June 17, 2021): 347. http://dx.doi.org/10.3390/md19060347.

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For utilizing the largest source of marine proteins, Antarctic krill (Euphausia superba) proteins were defatted and hydrolyzed separately using pepsin, alcalase, papain, trypsin, and netrase, and alcalase hydrolysate (EPAH) showed the highest DPPH radical (DPPH·) and hydroxyl radical (HO·) scavenging activity among five hydrolysates. Using ultrafiltration and chromatography methods, fifteen antioxidant peptides were purified from EPAH and identified as Asn-Gln-Met (NQM), Trp-Phe-Pro-Met (WFPM), Gln-Asn-Pro-Thr (QNPT), Tyr-Met-Asn-Phe (YMNF), Ser-Gly-Pro-Ala (SGPA), Ser-Leu-Pro-Tyr (SLPY), Gln-Tyr-Pro-Pro-Met-Gln-Tyr (QYPPMQY), Glu-Tyr-Glu-Ala (EYEA), Asn-Trp-Asp-Asp-Met-Arg-Ile-Val-Ala-Val (NWDDMRIVAV), Trp-Asp-Asp-Met-Glu-Arg-Leu-Val-Met-Ile (WDDMERLVMI), Asn-Trp-Asp-Asp-Met-Glu-Pro-Ser-Phe (NWD-DMEPSF), Asn-Gly-Pro-Asp-Pro-Arg-Pro-Ser-Gln-Gln (NGPDPRPSQQ), Ala-Phe-Leu-Trp-Asn (AFLWA), Asn-Val-Pro-Asp-Met (NVPDM), and Thr-Phe-Pro-Ile-Tyr-Asp-Tyr-Pro-Gln (TFPIYDPQ), respectively, using a protein sequencer and ESI/MS. Among fifteen antioxidant peptides, SLPY, QYPPMQY and EYEA showed the highest scavenging activities on DPPH· (EC50 values of 1.18 ± 0.036, 1.547 ± 0.150, and 1.372 ± 0.274 mg/mL, respectively), HO· (EC50 values of 0.826 ± 0.027, 1.022 ± 0.058, and 0.946 ± 0.011 mg/mL, respectively), and superoxide anion radical (EC50 values of 0.789 ± 0.079, 0.913 ± 0.007, and 0.793 ± 0.056 mg/mL, respectively). Moreover, SLPY, QYPPMQY and EYEA showed strong reducing power, protective capability against H2O2-damaged plasmid DNA, and lipid peroxidation inhibition ability. Furthermore, SLPY, QYPPMQY, and EYEA had high stability under temperatures lower than 80 °C, pH values ranged from 6–8, and simulated GI digestion for 180 min. The results showed that fifteen antioxidant peptides from alcalase hydrolysate of Antarctic krill proteins, especially SLPY, QYPPMQY and EYEA, might serve as effective antioxidant agents applied in food and health products.
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48

Lau, HK. "Anticoagulant function of a 24-Kd fragment isolated from human fibrinogen A alpha chains." Blood 81, no. 12 (June 15, 1993): 3277–84. http://dx.doi.org/10.1182/blood.v81.12.3277.3277.

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Abstract A fibrinogen fragment obtained by limited-plasmin proteolysis has been isolated and purified to apparent homogeneity by gel filtrations. This fragment, denoted as 24-Kd fragment, has an apparent M(r) approximately 24,000 and contains an N-terminal sequence of met-glu-leu-glu-arg-pro- gly-gly-asn-glu-ile. The fragment contains a large number of acidic amino acid residues, and its amino acid composition is similar to several fibrinogen A alpha chains degradation fragments isolated previously. It corresponds to a peptide of the fibrinogen A alpha chains, the N-terminal of which starts at alpha Met-240. This peptide delays thrombin plasma clotting time. It does not bind calcium ions and does not inhibit thrombin's amidolytic activity. It binds to immobilized fibrin but not fibrinogen. It also inhibits the polymerization of desAA and desAABB fibrin monomers by simultaneously decreasing the maximum rate and the maximum level of the polymerization reaction. However, the initial lag period of this reaction is not affected by the fragment.
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49

Hlaváček, Jan, Václav Čeřovský, Jana Pírková, Pavel Majer, Lenka Maletínská, and Jiřina Slaninová. "Analogues of the cholecystokinin octapeptide modified in the central part of the molecule." Collection of Czechoslovak Chemical Communications 56, no. 9 (1991): 1963–70. http://dx.doi.org/10.1135/cccc19911963.

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In a series of analogues of the cholecystokinin octapeptide (CCK-8) the amino acid residues were gradually modified by substituting Gly by Pro in position 4, Trp by His in position 5, Met by Cle in position 6, or the Gly residue was inserted between Tyr and Met in positions 2 and 3 of the peptide chain, and in the case of the cholecystokinin heptapeptide (CCK-7) the Met residues were substituted by Nle or Aib. These peptides were investigated from the point of view of their biological potency in the peripheral and central region. From the results of the biological tests it follows that the modifications carried out in these analogues and in their Nα-Boc derivatives mean a suppression of the investigated biological activities by 2-3 orders of magnitude (at a maximum dose of the tested substance of 2 . 10-2 mg per animal).This means that a disturbance of the assumed biologically active conformation of CCK-8, connected with a considerable decrease of the biological potency of the molecule, takes place not only after introduction of the side chain into its centre (substitution of Gly4), but also after the modification of the side chains of the amino acids or by extension of the backbone in further positions around this central amino acid.
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50

Mukai, H., K. Kawai, S. Suzuki, H. Ohmori, K. Yamashita, and E. Munekata. "[Ala6]gastrin-releasing peptide-10: an analogue with dissociated biological activities." American Journal of Physiology-Endocrinology and Metabolism 257, no. 2 (August 1, 1989): E235—E240. http://dx.doi.org/10.1152/ajpendo.1989.257.2.e235.

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COOH-terminal decapeptide of gastrin-releasing peptide (GRP-10) is a bombesin-like peptide, which has bioactivities to stimulate gastrin, insulin, and glucagon secretion. We have synthesized an analogue of GRP-10 that inhibits GRP-10's stimulation of insulin secretion both in vivo and in vitro and glucagon secretion in vivo, while potentiating the stimulation of gastrin secretion. The amino acid sequence of this peptide is H-Gly-Asn-Trp-Ala-Ala-Gly-His-Leu-Met-NH2 ([Ala6]GRP-10). Because the stimulation of insulin and gastrin secretion by GRP-10 has been ascribed to a direct effect on B- and G-cells, these findings suggest that there are two subtypes of receptors for bombesin-like peptides in mammalian tissues.
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