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Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain
The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 of the ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of the SARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connected b...
Autores principales: | , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Pleiades Publishing
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9798946/ https://www.ncbi.nlm.nih.gov/pubmed/36580213 http://dx.doi.org/10.1134/S1607672922060126 |
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author | Sidorova, M. V. Bibilashvili, R. S. Avdeev, D. V. Kozhokar, U. S. Palkeeva, M. E. Ovchinnikov, M. V. Molokoedov, A. S. Shirokov, D. A. Semyonova, A. V. Uvarova, V. I. Kulyaev, P. O. Khvatov, E. V. Ignatova, A. A. Feofanov, A. V. Osolodkin, D. I. Porozov, Yu. B. Kozlovskaya, L. I. Ishmukhametov, A. A. Parfyonova, Ye. V. Egorov, A. M. |
author_facet | Sidorova, M. V. Bibilashvili, R. S. Avdeev, D. V. Kozhokar, U. S. Palkeeva, M. E. Ovchinnikov, M. V. Molokoedov, A. S. Shirokov, D. A. Semyonova, A. V. Uvarova, V. I. Kulyaev, P. O. Khvatov, E. V. Ignatova, A. A. Feofanov, A. V. Osolodkin, D. I. Porozov, Yu. B. Kozlovskaya, L. I. Ishmukhametov, A. A. Parfyonova, Ye. V. Egorov, A. M. |
author_sort | Sidorova, M. V. |
collection | PubMed |
description | The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 of the ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of the SARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connected by disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide helicity were experimentally measured, and molecular dynamics simulation was performed in various solvents. It was established that the preservation of the helical conformation is a necessary condition for the binding of peptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric peptides have a higher degree of helicity than monomeric ones, probably due to the mutual influence of helices. The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the most suitable solvent is a water-ethanol mixture. |
format | Online Article Text |
id | pubmed-9798946 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Pleiades Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-97989462022-12-30 Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain Sidorova, M. V. Bibilashvili, R. S. Avdeev, D. V. Kozhokar, U. S. Palkeeva, M. E. Ovchinnikov, M. V. Molokoedov, A. S. Shirokov, D. A. Semyonova, A. V. Uvarova, V. I. Kulyaev, P. O. Khvatov, E. V. Ignatova, A. A. Feofanov, A. V. Osolodkin, D. I. Porozov, Yu. B. Kozlovskaya, L. I. Ishmukhametov, A. A. Parfyonova, Ye. V. Egorov, A. M. Dokl Biochem Biophys Biochemistry, Biophysics, and Molecular Biology The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 of the ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of the SARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connected by disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide helicity were experimentally measured, and molecular dynamics simulation was performed in various solvents. It was established that the preservation of the helical conformation is a necessary condition for the binding of peptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric peptides have a higher degree of helicity than monomeric ones, probably due to the mutual influence of helices. The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the most suitable solvent is a water-ethanol mixture. Pleiades Publishing 2022-12-29 2022 /pmc/articles/PMC9798946/ /pubmed/36580213 http://dx.doi.org/10.1134/S1607672922060126 Text en © The Author(s) 2022, ISSN 1607-6729, Doklady Biochemistry and Biophysics, 2022, Vol. 507, pp. 237–241. © The Author(s), 2022. This article is an open access publication.ISSN 1607-6729, Doklady Biochemistry and Biophysics, 2022. © The Author(s), 2022. This article is an open access publication.Russian Text © The Author(s), 2022, published in Doklady Rossiiskoi Akademii Nauk. Nauki o Zhizni, 2022, Vol. 507, pp. 455–459. https://creativecommons.org/licenses/by/4.0/Open Access.This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Biochemistry, Biophysics, and Molecular Biology Sidorova, M. V. Bibilashvili, R. S. Avdeev, D. V. Kozhokar, U. S. Palkeeva, M. E. Ovchinnikov, M. V. Molokoedov, A. S. Shirokov, D. A. Semyonova, A. V. Uvarova, V. I. Kulyaev, P. O. Khvatov, E. V. Ignatova, A. A. Feofanov, A. V. Osolodkin, D. I. Porozov, Yu. B. Kozlovskaya, L. I. Ishmukhametov, A. A. Parfyonova, Ye. V. Egorov, A. M. Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title | Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title_full | Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title_fullStr | Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title_full_unstemmed | Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title_short | Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain |
title_sort | properties and activity of peptide derivatives of ace2 cellular receptor and their interaction with sars-cov-2 s protein receptor-binding domain |
topic | Biochemistry, Biophysics, and Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9798946/ https://www.ncbi.nlm.nih.gov/pubmed/36580213 http://dx.doi.org/10.1134/S1607672922060126 |
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