Aydar A. Ishmukhametov
Research Subjects
Aydar A. Ishmukhametov has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Alina E. Ershova
Division of Immunobiology and Biomedicine, Sirius University of Science and Technology, 354349 Sirius, Russia
1 shared publication - Irina V. Astrakhantseva
Department of Immunobiology and Biomedicine, Sirius University of Science and Technology, 354349 Sirius, Krasnodarsky Krai, Russia
1 shared publication - Liubov I. Kozlovskaya
Federal State Autonomous Scientific Institution “Chumakov Federal Center for Research and Development of Immune-and-Biological Products of the Russian Academy of Sciences” (Institute of Poliomyelitis) (FSASI “Chumakov FSC R&D IBP RAS”), 108819 Moscow, Russia
1 shared publication - Marina S. Drutskaya
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences
1 shared publication - Natalia A. Kruglova
Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Institute of Gene Biology, Russian Academy of Sciences
1 shared publication - Sergei A. Chuvpilo
Division of Immunobiology and Biomedicine, Sirius University of Science and Technology, Sirius, Krasnodarsky Krai, 354349 Sochi, Russia
1 shared publication
Latest Publications
- Open Access
- 5 May 2023
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 24 (9) , 8269
SARS-CoV-2 Binding and Neutralization Properties of Peptides Derived from N-Terminus of Human ACE2
The binding properties of synthetic and recombinant peptides derived from N-terminal part of ACE2, the main receptor for SARS-CoV-2, were evaluated. Additionally, the ability of these peptides to prevent virus entry in vitro was addressed using both pseudovirus particles decorated with the S protein, as well as through infection of Vero cells with live SARS-CoV-2 virus. Surprisingly, in spite of effective binding to S protein, all linear peptides of various lengths failed to neutralize the viral infection in vitro. However, the P1st peptide that was chemically “stapled” in order to stabilize its alpha-helical structure was able to interfere with virus entry into ACE2-expressing cells. Interestingly, this peptide also neutralized pseudovirus particles decorated with S protein derived from the Omicron BA.1 virus, in spite of variations in key amino acid residues contacting ACE2.
- 5 May 2023
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 24 (9) , 8269
Open AccessSARS-CoV-2 Binding and Neutralization Properties of Peptides Derived from N-Terminus of Human ACE2
The binding properties of synthetic and recombinant peptides derived from N-terminal part of ACE2, the main receptor for SARS-CoV-2, were evaluated. Additionally, the ability of these peptides to prevent virus entry in vitro was addressed using both pseudovirus particles decorated with the S protein, as well as through infection of Vero cells with live SARS-CoV-2 virus. Surprisingly, in spite of effective binding to S protein, all linear peptides of various lengths failed to neutralize the viral infection in vitro. However, the P1st peptide that was chemically “stapled” in order to stabilize its alpha-helical structure was able to interfere with virus entry into ACE2-expressing cells. Interestingly, this peptide also neutralized pseudovirus particles decorated with S protein derived from the Omicron BA.1 virus, in spite of variations in key amino acid residues contacting ACE2.