Journal Article

SARS-CoV-2 Binding and Neutralization Properties of Peptides Derived from N-Terminus of Human ACE2

Ershova, Alina E., Nedospasov, Sergei A., Ishmukhametov, Aydar A., Drutskaya, Marina S., Chuvpilo, Sergei A., Kruglova, Natalia A., Astrakhantseva, Irina V., Kozlovskaya, Liubov I.

2023

Overview

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.

• Publisher: MDPI AG,MDPI
• Subject: Amino acids / Analysis / Angiotensin-Converting Enzyme 2 - metabolism / Animals / Chlorocebus aethiops / Coronaviruses / COVID-19 / Health aspects / Humans / Infections / Peptides / Peptides - metabolism / Peptides - pharmacology / Protein Binding / Proteins / SARS-CoV-2 - metabolism / Severe acute respiratory syndrome coronavirus 2 / Vero Cells / Viral infections / Virus diseases