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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 Domainстатья
- Авторы: 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.
- Журнал: Doklady Biochemistry and Biophysics
- Том: 507
- Год издания: 2022
- Издательство: M A I K Nauka - Interperiodica
- Местоположение издательства: Russian Federation
- Первая страница: 455
- Последняя страница: 459
- DOI: 10.1134/s1607672922060126
- Аннотация: The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 ofthe ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of theSARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connectedby disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide heli-city were experimentally measured, and molecular dynamics simulation was performed in various solvents. Itwas established that the preservation of the helical conformation is a necessary condition for the binding ofpeptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric pep-tides have a higher degree of helicity than monomeric ones, probably due to the mutual inf luence of helices.The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the mostsuitable solvent is a water-ethanol mixture.
- Добавил в систему: Уварова Виктория Игоревна