Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A series of monopyrrolinone-based HIV-1 protease inhibitors possessing rationally designed P2' side chains have been synthesized and evaluated for activity against wild-type HIV-1 protease. The most potent inhibitor displays subnanomolar potency in vitro for the wild-type HIV-1 protease. Additionally, the monopyrrolinone inhibitors retain potency in cellular assays against clinically significant mutant forms of the virus. X-ray structures of these inhibitors bound in the wild-type enzyme reveal important insights into the observed biological activity.
Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors possessing augmented P2' side chains.,Smith AB 3rd, Charnley AK, Harada H, Beiger JJ, Cantin LD, Kenesky CS, Hirschmann R, Munshi S, Olsen DB, Stahlhut MW, Schleif WA, Kuo LC Bioorg Med Chem Lett. 2006 Feb 15;16(4):859-63. Epub 2005 Nov 18. PMID:16298527[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Smith AB 3rd, Charnley AK, Harada H, Beiger JJ, Cantin LD, Kenesky CS, Hirschmann R, Munshi S, Olsen DB, Stahlhut MW, Schleif WA, Kuo LC. Design, synthesis, and biological evaluation of monopyrrolinone-based HIV-1 protease inhibitors possessing augmented P2' side chains. Bioorg Med Chem Lett. 2006 Feb 15;16(4):859-63. Epub 2005 Nov 18. PMID:16298527 doi:10.1016/j.bmcl.2005.11.011
