Pharmacology complex compound of pro-gly-pro-leu with heparin: hypoglycemic, fibrinolitic and anticoagulant effects in rats with hyperglycemia

Оберган, Т.Ю.; Мясоедов, Н.Ф.; Григорьева, М.Е.; Ляпина, Л.А.; Shubina, T. A.; Андреева, Л. А.

doi:10.19163/2307-9266-2019-7-5-300-307

Cited by 1 publication

(1 citation statement)

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“…Such a pharmacological agent is 11-amino acid peptide pHB-SP (PubChem CID: 91810664), which is an amino acid chain QEQLERALNSS (Pyr-Glu-Gln-Leu-Glu-Arg-Ala-Leu-Asn-Ser-Ser), having a selective affinity for the heterodimer complex EPOR/CD131 (Hache et al 2016). The short peptide chain allows its modification by adding the polypeptide motifs RGD (Arg-Gly-Asp), KGD (Lys-Gly-Asp) and PGP (Pro-Gly-Pro), which are known for their anti-aggregation properties (Pastorova et al 2001;Lyapina et al 2007;Liapina et al 2010;Obergan et al 2019;Kuo et al 2019). The key issue remains the retention of protective properties of innovative peptides mimicking the tertiary structure of the α-helix B of erythropoietin after embedding RGD, KGD and PGP motifs into the base molecule.…”

Section: Introductionmentioning

confidence: 99%

Preclinical study of innovative peptides mimicking the tertiary structure of the α-helix B of erythropoietin

Golubev¹,

Гуреев²,

Корокин³

et al. 2020

RRP

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Introduction: The aim of this study was to examine the effectiveness of innovative peptides obtained by addition of polypeptide motifs with antiaggregation activity (Arg-Gly-Asp, Lys-Gly-Asp and Pro-Gly-Pro) to a peptide mimicking the space structure of the α-helix B of erythropoietin pHBSP (Pyr-Glu-Gln-Leu-Glu-Arg-Ala-Leu-Asn-Ser-Ser). Materials and methods: The cytoprotective activity of innovative peptides mimicking the space structure of the α-helix B of erythropoietin at the doses of 5 μg/ml, 30 μg/ml and 50 μg/ml was studied on human endothelial cell culture in a simulated oxidative stress. An ADMA-like model of preeclampsia was simulated in the experiment. The study was conducted in 260 female Wistar rats, weighing 250–300 g. Results and discussion: Innovative peptides mimicking the space structure of the α-helix B of erythropoietin retain their cytoprotective activity in a simulated oxidative stress in HUVEC cell culture at the doses of 5 μg/ml, 30 μg/ml, and 50 μg/ml. The compounds with laboratory codes P-αB1 and P-αB3 had the most pronounced cytoprotective activity. Administration of N-nitro-L-arginine-methyl ether to pregnant females for 7 days causes the morphofunctional changes similar to clinical changes in preeclampsia. The innovative peptide under laboratory code P-αB4 at the dose of 50 μg/kg mimicking the space structure of the α-helix B of erythropoietin shows the most pronounced protective properties. Conclusion: Innovative peptides mimicking the space structure of the α-helix B of erythropoietin have a pronounced positive influence on the morphofunctional disorders in animals with ADMA-like preeclampsia.

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