کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1379239 | 982022 | 2006 | 5 صفحه PDF | دانلود رایگان |

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.
A series of monopyrrolinone-based HIV-1 protease inhibitors were synthesized and evaluated for activity against wild-type and mutant forms of the virus. X-ray cocrystal structures provide insight into their potent activity.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 16, Issue 4, 15 February 2006, Pages 859–863