Structure-based design of irreversible, tripeptidyl human rhinovirus 3C protease inhibitors containing N-methyl amino acids. |
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| Authors: | P S Dragovich S E Webber T J Prins R Zhou J T Marakovits J G Tikhe S A Fuhrman A K Patick D A Matthews C E Ford E L Brown S L Binford J W Meador R A Ferre S T Worland |
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| Affiliation: | Agouron Pharmaceuticals, Inc., San Diego, CA 92121, USA. |
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| Abstract: | Tripeptide-derived molecules incorporating N-methyl amino acid residues and C-terminal Michael acceptor moieties were evaluated as irreversible inhibitors of the cysteine-containing human rhinovirus 3C protease (3CP). Such compounds displayed good 3CP inhibition activity (k(obs)/[I] up to 610,000 M(-1) s(-1)) and potent in vitro antiviral properties (EC50 approaching 0.03 microM) when tested against HRV serotype-14. |
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