3oyp

Publication Abstract from PubMed

Designing selective inhibitors of proteases has proven problematic, in part because pharmacophores that confer potency exploit the conserved catalytic apparatus. We developed a fundamentally different approach by designing irreversible inhibitors that target noncatalytic cysteines that are structurally unique to a target in a protein family. We have successfully applied this approach to the important therapeutic target HCV protease, which has broad implications for the design of other selective protease inhibitors.

Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine.,Hagel M, Niu D, St Martin T, Sheets MP, Qiao L, Bernard H, Karp RM, Zhu Z, Labenski MT, Chaturvedi P, Nacht M, Westlin WF, Petter RC, Singh J Nat Chem Biol. 2011 Jan;7(1):22-4. Epub 2010 Nov 28. PMID:21113170^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.