Design, synthesis, and evaluation of azapeptides as substrates and inhibitors for human rhinovirus 3C protease.
A series of azapeptides was prepared and assessed as inhibitors of the human rhinovirus 3C protease. Boc-VLFaQ-OPh was a slow-turnover substrate that gave transient (ca. 1-2 h) inhibition as it underwent hydrolysis. Boc-VLFaG-OPh gave very slow but essentially irreversible inhibition.
Venkatraman
S
S
Department of Medicinal Chemistry, The University of Kansas, Lawrence 66045-2506, USA.
Kong
J
J
Nimkar
S
S
Wang
Q M
QM
Aubé
J
J
Hanzlik
R P
RP
D000086042:3C Viral Proteases; D001372:Aza Compounds / Q000737:chemistry*; D003546:Cysteine Endopeptidases / Q000187:drug effects*; D015853:Cysteine Proteinase Inhibitors / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D015195:Drug Design; D006868:Hydrolysis; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D013379:Substrate Specificity; D014764:Viral Proteins
D001372:Aza Compounds; D015853:Cysteine Proteinase Inhibitors; D010455:Peptides; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases