SARS-CoV-2 Binding and Neutralization Properties of Peptides Derived from N-Terminus of Human ACE2.
Irina V AstrakhantsevaAlina E ErshovaSergei A ChuvpiloNatalia A KruglovaAydar A IshmukhametovMarina S DrutskayaLiubov I KozlovskayaSergei A NedospasovPublished in: International journal of molecular sciences (2023)
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.
Keyphrases
- amino acid
- sars cov
- induced apoptosis
- angiotensin converting enzyme
- angiotensin ii
- respiratory syndrome coronavirus
- binding protein
- cell cycle arrest
- protein protein
- quantum dots
- endothelial cells
- endoplasmic reticulum stress
- reduced graphene oxide
- gold nanoparticles
- induced pluripotent stem cells
- small molecule
- dna binding