Journal articles on the topic 'Metal-Chelating Peptide'
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Matsubara, Teruhiko, Yuko Hiura, and Katsuhiro Kawashiro. "Biocombinatorial Selection of Metal Ion-Chelating Peptides." International Journal of Modern Physics B 17, no. 08n09 (2003): 1324–28. http://dx.doi.org/10.1142/s0217979203018946.
Full textKani, Hatice K., Ebru K. Kocazorbaz, and Figen Zihnioglu. "Investigation and isolation of peptide based antiglycating agents from various sources." Turkish Journal of Biochemistry 44, no. 5 (2019): 699–705. http://dx.doi.org/10.1515/tjb-2018-0294.
Full textChan, Pei-Teng, Patricia Matanjun, Cahyo Budiman, Rossita Shapawi, and Jau-Shya Lee. "Novel Peptide Sequences with ACE-Inhibitory and Antioxidant Activities Derived from the Heads and Bones of Hybrid Groupers (Epinephelus lanceolatus × Epinephelus fuscoguttatus)." Foods 11, no. 24 (2022): 3991. http://dx.doi.org/10.3390/foods11243991.
Full textDaubit, Isabelle Marie, and Nils Metzler-Nolte. "On the interaction of N-heterocyclic carbene Ir+I complexes with His and Cys containing peptides." Dalton Transactions 48, no. 36 (2019): 13662–73. http://dx.doi.org/10.1039/c9dt01338e.
Full textSmith, M. C., T. C. Furman, J. A. Cook, T. Ingolia, and H. Hsiung. "Chelating peptide-immobilized metal ion affinity chromatography." Journal of Inorganic Biochemistry 36, no. 3-4 (1989): 277. http://dx.doi.org/10.1016/0162-0134(89)84385-5.
Full textAlies, Bruno, Jacob D. Wiener, and Katherine J. Franz. "A prochelator peptide designed to use heterometallic cooperativity to enhance metal ion affinity." Chemical Science 6, no. 6 (2015): 3606–10. http://dx.doi.org/10.1039/c5sc00602c.
Full textIrankunda, Rachel, Jairo Andrés Camaño Echavarría, Cédric Paris, et al. "Metal-Chelating Peptides Separation Using Immobilized Metal Ion Affinity Chromatography: Experimental Methodology and Simulation." Separations 9, no. 11 (2022): 370. http://dx.doi.org/10.3390/separations9110370.
Full textLuisi, Grazia, Azzurra Stefanucci, Gokhan Zengin, Marilisa Dimmito, and Adriano Mollica. "Anti-Oxidant and Tyrosinase Inhibitory In Vitro Activity of Amino Acids and Small Peptides: New Hints for the Multifaceted Treatment of Neurologic and Metabolic Disfunctions." Antioxidants 8, no. 1 (2018): 7. http://dx.doi.org/10.3390/antiox8010007.
Full textLupaescu, Ancuta-Veronica, Ion Sandu, Brindusa Alina Petre, Laura Ion, Catalina-Ionica Ciobanu, and Gabi Drochioiu. "NAP Neuroprotective Peptide and its Analogs: Simultaneously Copper and Iron Binding and Reduction." Revista de Chimie 70, no. 5 (2019): 1784–90. http://dx.doi.org/10.37358/rc.19.5.7215.
Full textDayob, Kenana, Aygul Zengin, Ruslan Garifullin, et al. "Metal-Chelating Self-Assembling Peptide Nanofiber Scaffolds for Modulation of Neuronal Cell Behavior." Micromachines 14, no. 4 (2023): 883. http://dx.doi.org/10.3390/mi14040883.
Full textKrasae, K., W. Worawattanamateekul, and J. HInsui. "Effects of peptide fractions and amino acids on antioxidant properties of autolyzed tuna viscera protein hydrolysate." Food Research 7, no. 5 (2023): 156–63. http://dx.doi.org/10.26656/fr.2017.7(5).270.
Full textChen, Lei, Xuanri Shen, and Guanghua Xia. "Effect of Molecular Weight of Tilapia (Oreochromis Niloticus) Skin Collagen Peptide Fractions on Zinc-Chelating Capacity and Bioaccessibility of the Zinc-Peptide Fractions Complexes in Vitro Digestion." Applied Sciences 10, no. 6 (2020): 2041. http://dx.doi.org/10.3390/app10062041.
Full textKocadağ Kocazorbaz, Ebru. "Exploring the Functional Potential of Breast Milk Protein Hydrolysates: Antiglycation, Antioxidant, Metal Chelation, and Lipid Peroxidation Activities." Sakarya University Journal of Science 28, no. 6 (2024): 1178–87. http://dx.doi.org/10.16984/saufenbilder.1494769.
Full textIrankunda, Rachel, Jairo Andrés Camaño Echavarría, Cédric Paris, et al. "Deciphering Interactions Involved in Immobilized Metal Ion Affinity Chromatography and Surface Plasmon Resonance for Validating the Analogy between Both Technologies." Inorganics 12, no. 1 (2024): 31. http://dx.doi.org/10.3390/inorganics12010031.
Full textThompson, Channing C., and Rebecca Y. Lai. "Threonine Phosphorylation of an Electrochemical Peptide-Based Sensor to Achieve Improved Uranyl Ion Binding Affinity." Biosensors 12, no. 11 (2022): 961. http://dx.doi.org/10.3390/bios12110961.
Full textMagrì, Antonio, Diego La Mendola, and Enrico Rizzarelli. "Nerve Growth Factor Peptides Bind Copper(II) with High Affinity: A Thermodynamic Approach to Unveil Overlooked Neurotrophin Roles." International Journal of Molecular Sciences 22, no. 10 (2021): 5085. http://dx.doi.org/10.3390/ijms22105085.
Full textMeiss, Cade J., Paige J. Bothwell, and Michael I. Webb. "Ruthenium(II)–arene complexes with chelating quinoline ligands as anti-amyloid agents." Canadian Journal of Chemistry 100, no. 1 (2022): 18–24. http://dx.doi.org/10.1139/cjc-2021-0180.
Full textIavorschi, Monica, Ancuța-Veronica Lupăescu, Laura Darie-Ion, Maria Indeykina, Gabriela Elena Hitruc, and Brîndușa Alina Petre. "Cu and Zn Interactions with Peptides Revealed by High-Resolution Mass Spectrometry." Pharmaceuticals 15, no. 9 (2022): 1096. http://dx.doi.org/10.3390/ph15091096.
Full textIrankunda, Rachel, Pauline Jambon, Alexandra Marc, Jairo Andrés Camaño Echavarría, Laurence Muhr, and Laetitia Canabady-Rochelle. "Simulation of Ni2+ Chelating Peptides Separation in IMAC: Prediction of Langmuir Isotherm Parameters from SPR Affinity Data." Processes 12, no. 3 (2024): 592. http://dx.doi.org/10.3390/pr12030592.
Full textSmith, Michele C., Thomas C. Furman, and Charles Pidgeon. "Immobilized iminodiacetic acid metal peptide complexes. Identification of chelating peptide purification handles for recombinant proteins." Inorganic Chemistry 26, no. 12 (1987): 1965–69. http://dx.doi.org/10.1021/ic00259a030.
Full textChunkao, Siriporn, Wirote Youravong, Chutha T. Yupanqui, Adeola M. Alashi, and Rotimi E. Aluko. "Structure and Function of Mung Bean Protein-Derived Iron-Binding Antioxidant Peptides." Foods 9, no. 10 (2020): 1406. http://dx.doi.org/10.3390/foods9101406.
Full textSonklin, Chanikan, Natta Laohakunjit, and Orapin Kerdchoechuen. "Assessment of antioxidant properties of membrane ultrafiltration peptides from mungbean meal protein hydrolysates." PeerJ 6 (July 27, 2018): e5337. http://dx.doi.org/10.7717/peerj.5337.
Full textBellotti, Denise, Cinzia Tocchio, Remo Guerrini, Magdalena Rowińska-Żyrek, and Maurizio Remelli. "Thermodynamic and spectroscopic study of Cu(ii) and Zn(ii) complexes with the (148–156) peptide fragment of C4YJH2, a putative metal transporter of Candida albicans." Metallomics 11, no. 12 (2019): 1988–98. http://dx.doi.org/10.1039/c9mt00251k.
Full textReutzel, Jan, Timm M. Diogo та Armin Geyer. "Reversible Folding of a β-Hairpin Peptide by a Metal-Chelating Amino Acid". Chemistry - A European Journal 23, № 35 (2017): 8450–56. http://dx.doi.org/10.1002/chem.201700698.
Full textBíró, Linda, András Ozsváth, Réka Kapitány, and Péter Buglyó. "Pd(II) Binding Strength of a Novel Ambidentate Dipeptide-Hydroxypyridinonate Ligand; A Solution Equilibrium Study." Molecules 27, no. 14 (2022): 4667. http://dx.doi.org/10.3390/molecules27144667.
Full textKaugarenia, Nastassia, Sophie Beaubier, Erwann Durand, et al. "Optimization of Selective Hydrolysis of Cruciferins for Production of Potent Mineral Chelating Peptides and Napins Purification to Valorize Total Rapeseed Meal Proteins." Foods 11, no. 17 (2022): 2618. http://dx.doi.org/10.3390/foods11172618.
Full textManhiani, Paljinder, Julie K. Northcutt, and Paul L. Dawson. "Comparative Study of Antioxidant Activity between Carnosine and Its Amino Acid Constituents." Journal of Food Research 12, no. 3 (2023): 69. http://dx.doi.org/10.5539/jfr.v12n3p69.
Full textCsire, Gizella, Laetitia Canabady-Rochelle, Marie-Christine Averlant-Petit, Katalin Selmeczi, and Loic Stefan. "Both metal-chelating and free radical-scavenging synthetic pentapeptides as efficient inhibitors of reactive oxygen species generation." Metallomics 12, no. 8 (2020): 1220–29. http://dx.doi.org/10.1039/d0mt00103a.
Full textIbáñez, Alfredo J., Alexander Muck, and Aleš Svatoš. "Metal-Chelating Plastic MALDI (pMALDI) Chips for the Enhancement of Phosphorylated-Peptide/Protein Signals." Journal of Proteome Research 6, no. 9 (2007): 3842–48. http://dx.doi.org/10.1021/pr070243r.
Full textMonney, Angèle, Flavia Nastri, and Martin Albrecht. "Peptide-tethered monodentate and chelating histidylidene metal complexes: synthesis and application in catalytic hydrosilylation." Dalton Transactions 42, no. 16 (2013): 5655. http://dx.doi.org/10.1039/c3dt50424g.
Full textCarrasco-Castilla, Janet, Alan Javier Hernández-Álvarez, Cristian Jiménez-Martínez, et al. "Antioxidant and metal chelating activities of peptide fractions from phaseolin and bean protein hydrolysates." Food Chemistry 135, no. 3 (2012): 1789–95. http://dx.doi.org/10.1016/j.foodchem.2012.06.016.
Full textPérez-Gálvez, Raúl, F. Javier Espejo-Carpio, Pedro J. García-Moreno, Antonio Guadix, and Emilia M. Guadix. "Processing of Tuna Head By-Products into Antioxidant Peptide Ingredients for Aquaculture Feeds." Antioxidants 14, no. 7 (2025): 770. https://doi.org/10.3390/antiox14070770.
Full textO.O., Odekanyin,, Oriyomi, V.O, Olubayo, T., and Okhuevbie, R. "In vitro Antioxidant Bioactivity of Enzymatically-Produced Tilapia zillii and Oreochromis niloticus Muscle Protein Hydrolysates: Potential Application in Health and Nutrition." Asian Journal of Research in Biochemistry 15, no. 3 (2025): 145–58. https://doi.org/10.9734/ajrb/2025/v15i3396.
Full textAndrikopoulos, Prokopis C., and Pavel Čabart. "The chromatin remodeler SMARCA5 binds to d-block metal supports: Characterization of affinities by IMAC chromatography and QM analysis." PLOS ONE 19, no. 10 (2024): e0309134. http://dx.doi.org/10.1371/journal.pone.0309134.
Full textCiaglia, Tania, Maria Rosaria Miranda, Simone Di Micco, et al. "Neuroprotective Potential of Indole-Based Compounds: A Biochemical Study on Antioxidant Properties and Amyloid Disaggregation in Neuroblastoma Cells." Antioxidants 13, no. 12 (2024): 1585. https://doi.org/10.3390/antiox13121585.
Full textKumar, Lakshmanan Vinoth, Robinson Jeyashakila, Sarojini A., Vignaesh Dhanabalan, and Marimuthu Manivannan. "In vitro bioaccessibility and antioxidant properties of unicorn leatherjacket fish (Aluterus monoceros) skin collagen peptides prepared using crude collagenase enzyme isolated from fish fins." Brazilian Journal of Development 10, no. 6 (2024): e70488. http://dx.doi.org/10.34117/bjdv10n6-029.
Full textKjærgaard, Kristian, Jack K. Sørensen, Mark A. Schembri, and Per Klemm. "Sequestration of Zinc Oxide by Fimbrial Designer Chelators." Applied and Environmental Microbiology 66, no. 1 (2000): 10–14. http://dx.doi.org/10.1128/aem.66.1.10-14.2000.
Full textFloresta, Giuseppe, George P. Keeling, Siham Memdouh, Levente K. Meszaros, Rafael T. M. de Rosales, and Vincenzo Abbate. "NHS-Functionalized THP Derivative for Efficient Synthesis of Kit-Based Precursors for 68Ga Labeled PET Probes." Biomedicines 9, no. 4 (2021): 367. http://dx.doi.org/10.3390/biomedicines9040367.
Full textZHANG, Fang L., and Patrick J. CASEY. "Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I." Biochemical Journal 320, no. 3 (1996): 925–32. http://dx.doi.org/10.1042/bj3200925.
Full textCaragounis, Aphrodite, Tai Du, Gulay Filiz та ін. "Differential modulation of Alzheimer's disease amyloid β-peptide accumulation by diverse classes of metal ligands". Biochemical Journal 407, № 3 (2007): 435–50. http://dx.doi.org/10.1042/bj20070579.
Full textNowak, J., and H. Tsai. "The yeast aminopeptidase Y." Canadian Journal of Microbiology 34, no. 2 (1988): 118–24. http://dx.doi.org/10.1139/m88-024.
Full textSmith, M. C., T. C. Furman, T. D. Ingolia, and C. Pidgeon. "Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins." Journal of Biological Chemistry 263, no. 15 (1988): 7211–15. http://dx.doi.org/10.1016/s0021-9258(18)68629-6.
Full textFamuwagun, Akinsola A., Adeola M. Alashi, Saka O. Gbadamosi, et al. "Effect of Protease Type and Peptide Size on the In Vitro Antioxidant, Antihypertensive and Anti-Diabetic Activities of Eggplant Leaf Protein Hydrolysates." Foods 10, no. 5 (2021): 1112. http://dx.doi.org/10.3390/foods10051112.
Full textAhmadi, Mahmoud Kamal, Samar Fawaz, Charles H. Jones, Guojian Zhang, and Blaine A. Pfeifer. "Total Biosynthesis and Diverse Applications of the Nonribosomal Peptide-Polyketide Siderophore Yersiniabactin." Applied and Environmental Microbiology 81, no. 16 (2015): 5290–98. http://dx.doi.org/10.1128/aem.01373-15.
Full textKreutzer, Martin F., Hirokazu Kage, Peter Gebhardt, et al. "Biosynthesis of a Complex Yersiniabactin-Like Natural Product via themicLocus in Phytopathogen Ralstonia solanacearum." Applied and Environmental Microbiology 77, no. 17 (2011): 6117–24. http://dx.doi.org/10.1128/aem.05198-11.
Full textHu, Yangfan, Huan Luo, Vasudeva Reddy Netala, He Li, Zhijun Zhang, and Tianyu Hou. "Comprehensive Review of Biological Functions and Therapeutic Potential of Perilla Seed Meal Proteins and Peptides." Foods 14, no. 1 (2024): 47. https://doi.org/10.3390/foods14010047.
Full textCendron, Andrea, Martina Chianese, Kamil Zarzycki, et al. "Chelating Properties of N6O-Donors Toward Cu(II) Ions: Speciation in Aqueous Environments and Catalytic Activity of the Dinuclear Complexes." Molecules 29, no. 23 (2024): 5708. https://doi.org/10.3390/molecules29235708.
Full textAmoscato, Andrew A., Damon A. Prenovitz, and Michael T. Lotze. "Rapid Extracellular Degradation of Synthetic Class I Peptides by Human Dendritic Cells." Journal of Immunology 161, no. 8 (1998): 4023–32. http://dx.doi.org/10.4049/jimmunol.161.8.4023.
Full textFashakin, Olumide Oluwatoyosi, Pipat Tangjaidee, Kridsada Unban, et al. "Isolation and Identification of Antioxidant Peptides Derived from Cricket (Gryllus bimaculatus) Protein Fractions." Insects 14, no. 8 (2023): 674. http://dx.doi.org/10.3390/insects14080674.
Full textGonzález-Ortega, Omar, and Roberto Guzmán. "Reversible Immobilization of Chelating Affinity Surfactants on Reversed Phase Adsorbents for Protein and Peptide Separations under Metal Affinity Chromatography." American Journal of Analytical Chemistry 05, no. 14 (2014): 932–44. http://dx.doi.org/10.4236/ajac.2014.514101.
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