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- W4386046892 abstract "The entry of the SARS-CoV-2 virus into a human host cell begins with the interaction between the viral spike protein (S protein) and human angiotensin-converting enzyme 2 (hACE2). Therefore, a possible strategy for the treatment of this infection is based on inhibiting the interaction of the two abovementioned proteins. Compounds that bind to the SARS-CoV-2 S protein at the interface with the alpha-1/alpha-2 helices of ACE2 PD Subdomain I are of particular interest. We present a stepwise optimisation of helical peptide foldamers containing trans-2-aminocylopentanecarboxylic acid residues as the folding-inducing unit. Four rounds of optimisation led to the discovery of an 18-amino-acid peptide with high affinity for the SARS-CoV-2 S protein (Kd = 650 nM) that inhibits this protein-protein interaction with IC50 = 1.3 µM. Circular dichroism and nuclear magnetic resonance studies indicated the helical conformation of this peptide in solution." @default.
- W4386046892 created "2023-08-23" @default.
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- W4386046892 date "2023-08-21" @default.
- W4386046892 modified "2023-10-02" @default.
- W4386046892 title "Peptide foldamer-based inhibitors of the SARS-CoV-2 S protein–human ACE2 interaction" @default.
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- W4386046892 doi "https://doi.org/10.1080/14756366.2023.2244693" @default.
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