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.
Top-30
Journals
1
|
|
Computers in Biology and Medicine
1 publication, 33.33%
|
|
International Journal of Molecular Sciences
1 publication, 33.33%
|
|
Russian Chemical Reviews
1 publication, 33.33%
|
|
1
|
Publishers
1
|
|
Elsevier
1 publication, 33.33%
|
|
MDPI
1 publication, 33.33%
|
|
Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii
1 publication, 33.33%
|
|
1
|
- We do not take into account publications without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.