title: Design, synthesis, and evaluation of azapeptides as substrates and inhibitors for human rhinovirus 3C protease.
abstract: 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.
authors: Department of Medicinal Chemistry, The University of Kansas, Lawrence 66045-2506, USA.
authors: S
authors: S
authors: Venkatraman
authors: J
authors: J
authors: Kong
authors: S
authors: S
authors: Nimkar
authors: Q M
authors: QM
authors: Wang
authors: J
authors: J
authors: Aubé
authors: R P
authors: RP
authors: Hanzlik
mesh_terms: 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
chemical_list: D001372:Aza Compounds; D015853:Cysteine Proteinase Inhibitors; D010455:Peptides; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases