Yu. A. Pelogeykina

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Apelin-12 and a number of its analogues (Nle10-, MeArg1, Nle10, MeArg1, Nle10, Phe12-NH2-, Arg1(NO2), Nle10, Phe12-NH2-), resistant to the degradation of proteases, were synthesized by the Fmocmethod of SPPS. By-products of synthesis were examined. It was found that the serine hydroxyl group was sulfating during the final deprotection of apelin-12 and its(More)
This study investigated the effects of peptide apelin-12 (H-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe-OH, A12) and its novel structural analog (H-(NαMe)Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Nle-Pro-Phe-OH, AI) on myocardial antioxidant enzyme activities, lipid peroxidation, and reactive oxygen species formation in ex vivo and in vivo models of(More)
The adipocytokine apelin peptide, which consists of 77 amino acid residues, and its APJ receptor con nected with G proteins of membranes of endothelial cells and cardiomyocytes participate in regulation of the tone of coronary blood vessels and contractility of the myocardium [1]. C terminal fragments of the pep tide (apelin 12, 13, and 36) improve the(More)
Apelin-12 (A-12) peptide was synthesized by automated solid phase method and purified by reverse phase HPLC. Its homogeneity and structure were confirmed by HPLC, 1H-NMR spectroscopy, and mass spectroscopy. Acute myocardial infarction was induced by 40-min occlusion of the left coronary artery with subsequent 60-min reperfusion in narcotized Wistar rats.(More)
The effects of C-terminal fragment of natural peptide apelin-12 H-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Met-Pro-Phe-OH (A12) and its structural analog H-(NαMe)Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-Pro-Nle-Pro-Phe-OH (AI) on Cu2+-induced free radical oxidation of low-density lipoprotein in human blood plasma and activity of commercially available enzymes superoxide(More)
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