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Journal articles on the topic 'Histidine dipeptides'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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1

van Milgen, Jaap, and Nathalie Le Floc’h. "8 Functional Role of Histidine in Diets of Young Pigs." Journal of Animal Science 99, Supplement_1 (2021): 13. http://dx.doi.org/10.1093/jas/skab054.022.

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Abstract Histidine is a constituent amino acid of body proteins and, once incorporated in protein, histidine can be methylated post-translationally to methyl-histidine. Histidine is also a precursor of histamine, a neurotransmitter and involved in the immune response. Histidine and histamine are constituents of a number of dipeptides, which act as pH buffers, metal chelating agents, and anti-oxidants, especially in skeletal muscles and in the brain. A considerable fraction of whole-body histidine is present as carnosine, the dipeptide of histidine and β-alanine. In the longissimus muscle, about 40% of the total histidine content is present as carnosine. The histidine in carnosine can be methylated to anserine or balenine, and the pig is among the few species that synthesize both forms. Hydrolysis of body protein and of histidine-containing dipeptides results in the release of the constituent amino acids. However, only the histidine of protein and carnosine can be reused for protein synthesis. Methyl-histidine is either excreted in the urine or remains bound in the dipeptides and accumulates in the body. Because carnosine represents such a large histidine reservoir, a dietary histidine deficiency may not directly lead to a reduction in growth, especially if growth is given a higher priority for histidine utilization than maintaining or depleting the histidine-containing dipeptide reserves. Few histidine dose-response studies have been done in piglets and differences in the estimated requirements may be due to differences in diluting or depleting the dipeptide reserves. However, at low histidine intakes, both feed intake and growth are reduced and a reduction of the histidine-to-lysine supply by 1 percentage point results in a growth reduction of 4%. Histidine dose-response studies need to consider the role of histidine as a constituent amino acid of body protein as well as its role in dipeptides.
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2

Wang, Furong, Hailiang Shen, Ting Liu, Xi Yang, Yali Yang, and Yurong Guo. "Formation of Pyrazines in Maillard Model Systems: Effects of Structures of Lysine-Containing Dipeptides/Tripeptides." Foods 10, no. 2 (2021): 273. http://dx.doi.org/10.3390/foods10020273.

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At present, most investigations involving the Maillard reaction models have focused on free amino acids (FAAs), whereas the effects of peptides on volatile products are poorly understood. In our study, the formation mechanism of pyrazines, which were detected as characteristic volatiles in sunflower seed oil, from the reaction system of glucose and lysine-containing dipeptides and tripeptides was studied. The effect of the amino acid sequences of the dipeptides and tripeptides on pyrazine formation was further highlighted. Four different dipeptides and six tripeptides were selected. The results showed that the production of pyrazines in the lysine-containing dipeptide models was higher than that in the tripeptide and control models. Compounds 2,5(6)-Dimethylpyrazine and 2,3,5-trimethylpyrazine were the main pyrazine compounds in the dipeptide models. Furthermore, the C- or N-terminal amino acids of lysine-containing dipeptides can exert an important effect on the formation of pyrazines. In dipeptide models with lysine at the C-terminus, the content of total pyrazines followed the order of Arg−Lys > His−Lys; the order of the total pyrazine content was Lys−His > Lys−Arg in dipeptide models with N-terminal lysine. Additionally, for the tripeptide models with different amino acid sequences, more pyrazines and a greater variety of pyrazines were detected in the tripeptide models with N-terminal lysine/arginine than in the tripeptide models with N-terminal histidine. However, the total pyrazine content and the percentage of pyrazines in the total volatiles were similar in the tripeptide models with the same amino acids at the N-terminus. This study clearly illustrates the ability of dipeptides and tripeptides containing lysine, arginine and histidine to form pyrazines, improving volatile formation during sunflower seed oil processing.
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3

Heidenreich, Elena, Tilman Pfeffer, Tamara Kracke, et al. "A Novel UPLC-MS/MS Method Identifies Organ-Specific Dipeptide Profiles." International Journal of Molecular Sciences 22, no. 18 (2021): 9979. http://dx.doi.org/10.3390/ijms22189979.

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Background: Amino acids have a central role in cell metabolism, and intracellular changes contribute to the pathogenesis of various diseases, while the role and specific organ distribution of dipeptides is largely unknown. Method: We established a sensitive, rapid and reliable UPLC-MS/MS method for quantification of 36 dipeptides. Dipeptide patterns were analyzed in brown and white adipose tissues, brain, eye, heart, kidney, liver, lung, muscle, sciatic nerve, pancreas, spleen and thymus, serum and urine of C57BL/6N wildtype mice and related to the corresponding amino acid profiles. Results: A total of 30 out of the 36 investigated dipeptides were detected with organ-specific distribution patterns. Carnosine and anserine were most abundant in all organs, with the highest concentrations in muscles. In liver, Asp-Gln and Ala-Gln concentrations were high, in the spleen and thymus, Glu-Ser and Gly-Asp. In serum, dipeptide concentrations were several magnitudes lower than in organ tissues. In all organs, dipeptides with C-terminal proline (Gly-Pro and Leu-Pro) were present at higher concentrations than dipeptides with N-terminal proline (Pro-Gly and Pro-Leu). Organ-specific amino acid profiles were related to the dipeptide profile with several amino acid concentrations being related to the isomeric form of the dipeptides. Aspartate, histidine, proline and serine tissue concentrations correlated with dipeptide concentrations, when the amino acids were present at the C- but not at the N-terminus. Conclusion: Our multi-dipeptide quantification approach demonstrates organ-specific dipeptide distribution. This method allows us to understand more about the dipeptide metabolism in disease or in healthy state.
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4

Skopicki, H. A., K. Fisher, D. Zikos, et al. "Carrier-mediated transport of pyroglutamyl-histidine in renal brush border membrane vesicles." American Journal of Physiology-Cell Physiology 255, no. 6 (1988): C822—C827. http://dx.doi.org/10.1152/ajpcell.1988.255.6.c822.

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These studies were performed to determine if a transmembrane carrier for pyroglutamyl-histidine (pGlu-His) is present in the luminal membrane of renal proximal tubular cells. Previous studies have suggested the intact transepithelial transport of pGlu-His, a dipeptide formed by the hydrolysis of luteinizing hormone-releasing hormone by enzymes associated with the brush border in the proximal nephron. With the use of a renal brush border membrane vesicle preparation, pGlu-His showed H+-stimulated, Na-independent, saturable transport into an osmotically active space. High-pressure liquid chromatographic analysis of both the intravesicular and extravesicular fluids indicated intact uptake of the dipeptide. The transport constant (Kt) and Vmax for pGlu-His transport were 9.3 X 10(-8) M and 6.1 X 10(-12) mol.mg-1.min-1, respectively. Transport of pGlu-His was not inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and N-beta-alanyl-L-histidine, which have been previously shown to be transported into renal brush border vesicles via a single, low-affinity, high-capacity, Na-independent, and H+-stimulated peptide carrier. In addition, the gamma-glutamyl-containing peptides gamma-glutamyl-histidine and N(N-L-gamma-glutamyl-L-cysteinyl)glycine and the tripeptide pyroglutamyl-histidyl-prolinamide were without an inhibitory effect. In contrast, transport of pGlu-His was inhibited by the dipeptide pyroglutamyl-alanine. This study demonstrates the existence of a high-affinity, low-capacity H+ cotransport system for pGlu-His in the proximal tubular luminal plasmalemma, which appears to be specific for pyroglutamyl-containing dipeptides. The data indicate that multiple dipeptide carriers are present in the proximal nephron.
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5

Skopicki, H. A., K. Fisher, D. Zikos, G. Flouret, and D. R. Peterson. "Low-affinity transport of pyroglutamyl-histidine in renal brush-border membrane vesicles." American Journal of Physiology-Cell Physiology 257, no. 5 (1989): C971—C975. http://dx.doi.org/10.1152/ajpcell.1989.257.5.c971.

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These studies were performed to determine if a low-affinity carrier is present in the luminal membrane of proximal tubular cells for the transport of the dipeptide, pyroglutamyl-histidine (pGlu-His). We have previously described the existence of a specific, high-affinity, low-capacity [transport constant (Kt) = 9.3 X 10(-8) M, Vmax = 6.1 X 10(-12) mol.mg-1.min-1] carrier for pGlu-His in renal brush-border membrane vesicles. In the present study, we sought to demonstrate that multiple carriers exist for the transport of a single dipeptide by determining whether a low-affinity carrier also exists for the uptake of pGlu-His. Transport of pGlu-His into brush-border membrane vesicles was saturable over the concentration range of 10(-5)-10(-3) M, yielding a Kt of 6.3 X 10(-5) M and a Vmax of 2.2 X 10(-10) mol.mg-1.min-1. Uptake was inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and carnosine but not by the tripeptide pyroglutamyl-histidyl-prolinamide. We conclude that 1) pGlu-His is transported across the luminal membrane of the proximal tubule by multiple carriers and 2) the lower affinity carrier, unlike the higher affinity carrier, is nonspecific with respect to other dipeptides.
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6

Ferranco, Annaleizle, Shibaji Basak, Alan Lough, and Heinz-Bernhard Kraatz. "Metal coordination of ferrocene–histidine conjugates." Dalton Transactions 46, no. 14 (2017): 4844–59. http://dx.doi.org/10.1039/c7dt00456g.

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7

Baldwin, J. "Identification of histidine dipeptides in monotreme muscle." Biochemical Systematics and Ecology 23, no. 7-8 (1995): 869–70. http://dx.doi.org/10.1016/0305-1978(95)00073-9.

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8

Song, Byeng Chun, Nam-Seok Joo, Giancarlo Aldini, and Kyung-Jin Yeum. "Biological functions of histidine-dipeptides and metabolic syndrome." Nutrition Research and Practice 8, no. 1 (2014): 3. http://dx.doi.org/10.4162/nrp.2014.8.1.3.

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9

Barbaresi, Silvia, Luc Maertens, Erik Claeys, Wim Derave, and Stefaan De Smet. "Differences in muscle histidine‐containing dipeptides in broilers." Journal of the Science of Food and Agriculture 99, no. 13 (2019): 5680–86. http://dx.doi.org/10.1002/jsfa.9829.

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10

Zhu, Xiao-fei, Min Fan, Xu-bin Wang, et al. "Hydrolysis of DNA by a Dipeptides Containing Histidine." International Journal of Peptide Research and Therapeutics 16, no. 4 (2010): 297–300. http://dx.doi.org/10.1007/s10989-010-9232-x.

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11

Seo, Hyo-Suk, Seon-Yeong Kwak, and Yoon-Sik Lee. "Antioxidative activities of histidine containing caffeic acid-dipeptides." Bioorganic & Medicinal Chemistry Letters 20, no. 14 (2010): 4266–72. http://dx.doi.org/10.1016/j.bmcl.2010.04.135.

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12

Heyda, Jan, Philip E. Mason, and Pavel Jungwirth. "Attractive Interactions between Side Chains of Histidine-Histidine and Histidine-Arginine-Based Cationic Dipeptides in Water." Journal of Physical Chemistry B 114, no. 26 (2010): 8744–49. http://dx.doi.org/10.1021/jp101031v.

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13

Boldyrev, Alexander A., Giancarlo Aldini, and Wim Derave. "Physiology and Pathophysiology of Carnosine." Physiological Reviews 93, no. 4 (2013): 1803–45. http://dx.doi.org/10.1152/physrev.00039.2012.

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Carnosine (β-alanyl-l-histidine) was discovered in 1900 as an abundant non-protein nitrogen-containing compound of meat. The dipeptide is not only found in skeletal muscle, but also in other excitable tissues. Most animals, except humans, also possess a methylated variant of carnosine, either anserine or ophidine/balenine, collectively called the histidine-containing dipeptides. This review aims to decipher the physiological roles of carnosine, based on its biochemical properties. The latter include pH-buffering, metal-ion chelation, and antioxidant capacity as well as the capacity to protect against formation of advanced glycation and lipoxidation end-products. For these reasons, the therapeutic potential of carnosine supplementation has been tested in numerous diseases in which ischemic or oxidative stress are involved. For several pathologies, such as diabetes and its complications, ocular disease, aging, and neurological disorders, promising preclinical and clinical results have been obtained. Also the pathophysiological relevance of serum carnosinase, the enzyme actively degrading carnosine into l-histidine and β-alanine, is discussed. The carnosine system has evolved as a pluripotent solution to a number of homeostatic challenges. l-Histidine, and more specifically its imidazole moiety, appears to be the prime bioactive component, whereas β-alanine is mainly regulating the synthesis of the dipeptide. This paper summarizes a century of scientific exploration on the (patho)physiological role of carnosine and related compounds. However, far more experiments in the fields of physiology and related disciplines (biology, pharmacology, genetics, molecular biology, etc.) are required to gain a full understanding of the function and applications of this intriguing molecule.
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14

Ihara, Hideshi, Yuki Kakihana, Akane Yamakage, et al. "2-Oxo-histidine–containing dipeptides are functional oxidation products." Journal of Biological Chemistry 294, no. 4 (2018): 1279–89. http://dx.doi.org/10.1074/jbc.ra118.006111.

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15

Wieczorek, Rafał, Mark Dörr, Agata Chotera, Pier Luigi Luisi, and Pierre-Alain Monnard. "Formation of RNA Phosphodiester Bond by Histidine-Containing Dipeptides." ChemBioChem 14, no. 2 (2012): 217–23. http://dx.doi.org/10.1002/cbic.201200643.

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16

Ihara, Hideshi, Yuki Kakihana, Akane Yamakage, Takahiro Shibata, and Koji Uchida. "Detection and quantification of 2-oxo-histidine-containing dipeptides." Free Radical Biology and Medicine 112 (November 2017): 26–27. http://dx.doi.org/10.1016/j.freeradbiomed.2017.10.027.

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17

Mineeva, M. F., and S. L. Stvolinskii. "Effect of histidine-containing dipeptides on brain tyrosine hydroxylase." Bulletin of Experimental Biology and Medicine 121, no. 4 (1996): 382–84. http://dx.doi.org/10.1007/bf02446734.

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18

ZHAO, Yufen. "Discovery of Seryl-Histidine Dipeptide: From N-phosphoryl Amino Acids to Functional Dipeptides." University Chemistry 34, no. 12 (2019): 86–90. http://dx.doi.org/10.3866/pku.dxhx201911044.

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19

Masuoka, Nobutaka, Chenxu Lei, Haowei Li, and Tatsuhiro Hisatsune. "Influence of Imidazole-Dipeptides on Cognitive Status and Preservation in Elders: A Narrative Review." Nutrients 13, no. 2 (2021): 397. http://dx.doi.org/10.3390/nu13020397.

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The worldwide increase in the number of patients with dementia is becoming a growing problem, while Alzheimer’s disease (AD), a primary neurodegenerative disorder, accounts for more than 70% of all dementia cases. Research on the prevention or reduction of AD occurrence through food ingredients has been widely conducted. In particular, histidine-containing dipeptides, also known as imidazole dipeptides derived from meat, have received much attention. Imidazole dipeptides are abundant in meats such as poultry, fish, and pork. As evidenced by data from recent human intervention trials conducted worldwide, daily supplementation of carnosine and anserine, which are both imidazole dipeptides, can improve memory loss in the elderly and reduce the risk of developing AD. This article also summarizes the latest researches on the biochemical properties of imidazole dipeptides and their effects on animal models associated with age-related cognitive decline. In this review, we focus on the results of human intervention studies using supplements of poultry-derived imidazole dipeptides, including anserine and carnosine, affecting the preservation of cognitive function in the elderly, and discuss how imidazole dipeptides act in the brain to prevent age-related cognitive decline and the onset of dementia.
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20

Velíšek, J., R. Kubec, and K. Cejpek. "Biosynthesis of food constituents: Peptides – a review." Czech Journal of Food Sciences 24, No. 4 (2011): 149–55. http://dx.doi.org/10.17221/3311-cjfs.

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This review article gives a brief survey of principal pathways that lead to the biosynthesis of most important peptides occurring in foods. Glutathione, selected plant γ-glutamyl peptides, and animal histidine dipeptides are included in this review.    
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21

Kasziba, Eva, Louis Flancbaum, John C. Fitzpatrick, Joanna Schneiderman, and Hans Fisher. "Simultaneous determination of histidine-containing dipeptides, histamine, methylhistamine and histidine by high-performance liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 432 (January 1988): 315–20. http://dx.doi.org/10.1016/s0378-4347(00)80659-3.

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22

Tono-oka, Shuichi, Ichiro Azuma, Torunn Aakermann, et al. "Evidence for Enzymatic ADP-Ribosylation to Histidine and Related Dipeptides." Acta Chemica Scandinavica 48 (1994): 780–82. http://dx.doi.org/10.3891/acta.chem.scand.48-0780.

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23

Gockel, P., R. Vogler, M. Gelinsky, A. Meißner, H. Albrich, and H. Vahrenkamp. "Zinc complexation of cyclic dipeptides containing cysteine and/or histidine." Inorganica Chimica Acta 323, no. 1-2 (2001): 16–22. http://dx.doi.org/10.1016/s0020-1693(01)00561-8.

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24

Bokeriya, L. A., A. A. Boldyrev, R. R. Movsesyan, et al. "Cardioprotective effect of histidine-containing dipeptides in pharmacological cold cardioplegia." Bulletin of Experimental Biology and Medicine 145, no. 3 (2008): 323–27. http://dx.doi.org/10.1007/s10517-008-0081-y.

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25

Garribba, Eugenio, Elzbieta Lodyga-Chruscinska, Giovanni Micera, Angelo Panzanelli, and Daniele Sanna. "Binding of Oxovanadium(IV) to Dipeptides Containing Histidine and Cysteine Residues." European Journal of Inorganic Chemistry 2005, no. 7 (2005): 1369–82. http://dx.doi.org/10.1002/ejic.200400576.

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26

Vogler, Raphael, and Heinrich Vahrenkamp. "Dipeptides Made up Solely from Histidine: Solution Behaviour and Zinc Complexation." European Journal of Inorganic Chemistry 2002, no. 3 (2002): 761–66. http://dx.doi.org/10.1002/1099-0682(200203)2002:3<761::aid-ejic761>3.0.co;2-v.

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27

Boldyrev, A. A. "Retrospectives and perspectives on the biological activity of histidine-containing dipeptides." International Journal of Biochemistry 22, no. 2 (1990): 129–32. http://dx.doi.org/10.1016/0020-711x(90)90173-z.

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28

Boldyrev, A. A., A. M. Dupin, E. V. Pindel, and S. E. Severin. "Antioxidative properties of histidine-containing dipeptides from skeletal muscles of vertebrates." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 89, no. 2 (1988): 245–50. http://dx.doi.org/10.1016/0305-0491(88)90218-0.

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29

Tsogoeva, Svetlana B., and Shengwei Wei. "(S)-Histidine-based dipeptides as organic catalysts for direct asymmetric aldol reactions." Tetrahedron: Asymmetry 16, no. 11 (2005): 1947–51. http://dx.doi.org/10.1016/j.tetasy.2005.04.027.

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30

Boldyrev, Alexander A., and Sergei E. Severin. "The histidine-containing dipeptides, carnosine and anserine: Distribution, properties and biological significance." Advances in Enzyme Regulation 30 (1990): 175–94. http://dx.doi.org/10.1016/0065-2571(90)90017-v.

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31

Xie, Zhengzhi, Shahid P. Baba, Brooke R. Sweeney, and Oleg A. Barski. "Detoxification of aldehydes by histidine-containing dipeptides: From chemistry to clinical implications." Chemico-Biological Interactions 202, no. 1-3 (2013): 288–97. http://dx.doi.org/10.1016/j.cbi.2012.12.017.

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32

Hartman, Philip E., Zlata Hartman та Martin J. Citardi. "Ergothioneine, Histidine, and Two Naturally Occurring Histidine Dipeptides as Radioprotectors against γ-Irradiation Inactivation of Bacteriophages T4 and P22". Radiation Research 114, № 2 (1988): 319. http://dx.doi.org/10.2307/3577228.

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33

Kumagai, Momochika, Sanae Kato, Nanami Arakawa, et al. "Quantification of Histidine-Containing Dipeptides in Dolphin Serum Using a Reversed-Phase Ion-Pair High-Performance Liquid Chromatography Method." Separations 8, no. 8 (2021): 128. http://dx.doi.org/10.3390/separations8080128.

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The quantification of histidine-containing dipeptides (anserine, carnosine, and balenine) in serum might be a diagnostic tool to assess the health condition of animals. In this study, an existing reversed-phase ion-pair high-performance liquid chromatography (HPLC)–ultraviolet detection method was improved and validated to quantify serum anserine, carnosine, and balenine levels in the dolphin. The serum was deproteinized with trichloroacetic acid and directly injected into the HPLC system. Chromatographic separation of the three histidine-containing dipeptides was achieved on a TSK–gel ODS-80Ts (4.6 mm × 150 mm, 5 µm) analytical column using a mobile phase of 50 mmol/L potassium dihydrogen phosphate (pH 3.4) containing 6 mmol/L 1-heptanesulfonic acid and acetonitrile (96:4). The standard curve ranged from 0.1 µmol/L to 250 µmol/L. The average accuracy of the intra- and inter-analysis of anserine, carnosine, and balenine was 97–106%. The relative standard deviations of total precision (RSDr) of anserine, carnosine, and balenine in dolphin serum were 5.9%, 4.1%, and 2.6%, respectively. The lower limit of quantification of these compounds was 0.11–0.21 µmol/L. These results indicate that the improved method is reliable and concise for the simultaneous determination of anserine, carnosine, and balenine in dolphin serum, and may be useful for evaluation of health conditions in dolphins. Furthermore, this method can also be applied to other biological samples.
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34

Warżajtis, Beata, Biljana Đ. Glišić, Nada D. Savić, et al. "Mononuclear gold(iii) complexes withl-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion." Dalton Transactions 46, no. 8 (2017): 2594–608. http://dx.doi.org/10.1039/c6dt04862e.

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35

Peretto, Paolo, Federico Luzzati, Luca Bonfanti, Silvia De Marchis, and Aldo Fasolo. "Aminoacyl-histidine dipeptides in the glial cells of the adult rabbit forebrain☆,1." Peptides 21, no. 11 (2000): 1717–24. http://dx.doi.org/10.1016/s0196-9781(00)00322-3.

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36

Kang, Sohye, Johanna Mullen, Les P. Miranda, and Rohini Deshpande. "Utilization of tyrosine- and histidine-containing dipeptides to enhance productivity and culture viability." Biotechnology and Bioengineering 109, no. 9 (2012): 2286–94. http://dx.doi.org/10.1002/bit.24507.

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37

Vistoli, Giulio, Valentina Straniero, Alessandro Pedretti, et al. "Predicting the physicochemical profile of diastereoisomeric histidine-containing dipeptides by property space analysis." Chirality 24, no. 7 (2012): 566–76. http://dx.doi.org/10.1002/chir.22056.

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38

Oshima, Tatsuya, Toshihiko Sakamoto, Hodzumi Tachiyama, Kaoru Ohe, and Yoshinari Baba. "Adsorptive Recovery of Histidine-Containing Dipeptides Using Copper (II) Immobilized Cellulosic Chelating Adsorbent." KAGAKU KOGAKU RONBUNSHU 36, no. 3 (2010): 167–73. http://dx.doi.org/10.1252/kakoronbunshu.36.167.

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39

Cleij, Marco C., Wiendelt Drenth, and Roeland J. M. Nolte. "Mechanism of enantioselective ester cleavage by histidine containing dipeptides at a micellar interface." Journal of Organic Chemistry 56, no. 12 (1991): 3883–91. http://dx.doi.org/10.1021/jo00012a019.

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40

Liu, Jianbo, Fushi Zhang, Yu Zhao, Fuqun Zhao, Yingwu Tang, and Xinqi Song. "Influence of peptide bond on photosensitized oxidation of tryptophan, tyrosine and histidine dipeptides." Chinese Science Bulletin 42, no. 19 (1997): 1624–28. http://dx.doi.org/10.1007/bf02882572.

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41

GLIŠIĆ, BILJANA Đ., SNEŽANA RAJKOVIĆ, and MILOŠ I. DJURAN. "The reactions of [Au(dien)Cl]2+ with L-histidine-containing dipeptides. Dependence of complex formation on the dipeptide structure." Journal of Coordination Chemistry 66, no. 3 (2013): 424–34. http://dx.doi.org/10.1080/00958972.2012.759652.

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42

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 &lt; pH &lt; 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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43

Ichikawa, Kazuhiko, M. Khabir Uddin, and Kou Nakata. "Zinc Complexes of Artificial Histidine-containing Dipeptides as Catalysts of Hydrolyses ofp-Nitrophenyl Phosphates." Chemistry Letters 28, no. 2 (1999): 115–16. http://dx.doi.org/10.1246/cl.1999.115.

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44

Stegen, Sanne, Inge Everaert, Louise Deldicque, et al. "Muscle Histidine-Containing Dipeptides Are Elevated by Glucose Intolerance in Both Rodents and Men." PLOS ONE 10, no. 3 (2015): e0121062. http://dx.doi.org/10.1371/journal.pone.0121062.

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45

Wieczorek, Rafał, Mark Dörr, Agata Chotera, Pier Luigi Luisi, and Pierre-Alain Monnard. "Inside Cover: Formation of RNA Phosphodiester Bond by Histidine-Containing Dipeptides (ChemBioChem 2/2013)." ChemBioChem 14, no. 2 (2013): 166. http://dx.doi.org/10.1002/cbic.201390001.

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46

Oshima, Tatsuya, Kenzo Kanemaru, Hodzumi Tachiyama, Kaoru Ohe, and Yoshinari Baba. "Adsorption of histidine-containing dipeptides on copper(II) immobilized chelating resin from saline solution." Journal of Chromatography B 876, no. 1 (2008): 116–22. http://dx.doi.org/10.1016/j.jchromb.2008.10.039.

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47

Vaidyan, Alexander Varghese, and Pabitra K. Bhattacharya. "Interligand interaction in ternary complexes of Zn(II) and Cd(II) with dipeptides and aminoacids." Canadian Journal of Chemistry 72, no. 4 (1994): 1107–10. http://dx.doi.org/10.1139/v94-140.

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The stability constants of binary and ternary complexes [MA], [Ma2], and [MAL] (where M = Zn(II) or Cd(II); A = glycylglycine, glycyl L-alanine, glycyl L-leucine; L = α-alanine phenylalanine, tyrosine, tryptophan, or L-histidine) in aqueous medium have been determined potentometrically at 25 °C and an ionic strength of 0.2 M NaClO4 (0.2 mol dm−3) using a computer system. It is observed that Δ log K of MAL complexes has low negative or positive values. Probable reasons have been discussed.
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48

Hoetker, David, Weiliang Chung, Deqing Zhang та ін. "Exercise alters and β-alanine combined with exercise augments histidyl dipeptide levels and scavenges lipid peroxidation products in human skeletal muscle". Journal of Applied Physiology 125, № 6 (2018): 1767–78. http://dx.doi.org/10.1152/japplphysiol.00007.2018.

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Carnosine and anserine are dipeptides synthesized from histidine and β-alanine by carnosine synthase (ATPGD1). These dipeptides, present in high concentration in the skeletal muscle, form conjugates with lipid peroxidation products such as 4-hydroxy trans-2-nonenal (HNE). Although skeletal muscle levels of these dipeptides could be elevated by feeding β-alanine, it is unclear how these dipeptides and their conjugates are affected by exercise training with or without β-alanine supplementation. We recruited 20 physically active men, who were allocated to either β-alanine or placebo-feeding group matched for peak oxygen consumption, lactate threshold, and maximal power. Participants completed 2 wk of a conditioning phase followed by 1 wk of exercise training, a single session of high-intensity interval training (HIIT), followed by 6 wk of HIIT. Analysis of muscle biopsies showed that the levels of carnosine and ATPGD1 expression were increased after CPET and decreased following a single session and 6 wk of HIIT. Expression of ATPGD1 and levels of carnosine were increased upon β-alanine-feeding after CPET, whereas ATPGD1 expression decreased following a single session of HIIT. The expression of fiber type markers myosin heavy chain I and IIa remained unchanged after CPET. Levels of carnosine, anserine, carnosine-HNE, carnosine-propanal, and carnosine-propanol were further increased after 9 wk of β-alanine supplementation and exercise training but remained unchanged in the placebo-fed group. These results suggest that carnosine levels and ATPGD1 expression fluctuates with different phases of training. Enhancing carnosine levels by β-alanine feeding could facilitate the detoxification of lipid peroxidation products in the human skeletal muscle.NEW &amp; NOTEWORTHY Carnosine synthase expression and carnosine levels are altered in the human skeletal muscle during different phases of training. During high-intensity interval training, β-alanine feeding promotes detoxification of lipid peroxidation products and increases anserine levels in the skeletal muscle.
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49

Strašák, Milan, та Zlatica Durcová. "ESR study of the structure and bonding parameters in binary copper(II) complexes of some α-amino acids and dipeptides". Collection of Czechoslovak Chemical Communications 55, № 2 (1990): 546–54. http://dx.doi.org/10.1135/cccc19900546.

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Binary 1 : 1 copper(II)-amino acid and copper(II)-dipeptide complexes, [CuL] and [CuL]+ (H2L = +H3N-CHR-CO-NH-CHR'-COO-, HL' = +H3N-CHR-COO-), have been investigated in aqueous solution by means of ESR and electron absorption spectroscopy. Molecular orbital coefficients characteristic of the metal-ligand bonds have been derived for an effective D4h local symmetry. It is suggested that at the pH near to the physiological conditions both histidine and tryptophan coordinate as a tridentate ligand via O(carboxyl), N(heterocyclic ring) and N(amino) atoms. ESR investigation at room temperature and in frozen aqueous solutions, and visible spectral evidence suggest histamine-like coordination of histidine and tryptamine-like coordination of tryptophan in the quatorial plane of the binary complexes. Since proline contains the imino group, there is no ionizable amide-NH-proton when it is inserted in a peptide chain, hence the proline-nitrogen is unable to bind metal ions in peptides.
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50

Vistoli, Giulio, Mara Colzani, Angelica Mazzolari, et al. "Computational approaches in the rational design of improved carbonyl quenchers: focus on histidine containing dipeptides." Future Medicinal Chemistry 8, no. 14 (2016): 1721–37. http://dx.doi.org/10.4155/fmc-2016-0088.

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