Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (etravirine) and related non-nucleoside reverse transcriptase inhibitors that are highly potent and effective against wild-type and drug-resistant HIV-1 variants.

doi:10.1021/jm030558s

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Article

Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (etravirine) and related non-nucleoside reverse transcriptase inhibitors that are highly potent and effective against wild-type and drug-resistant HIV-1 variants.

Journal of medicinal chemistry - 6 May 2004

Das Kalyan, Clark Arthur D, Lewi Paul J, Heeres Jan, De Jonge Marc R, Koymans Lucien M H, Vinkers H Maarten, Daeyaert Frederik, Ludovici Donald W, Kukla Michael J, De Corte Bart, Kavash Robert W, Ho Chih Y, Ye Hong, Lichtenstein Mark A, Andries Koen, Pauwels Rudi, De Béthune Marie-Pierre, Boyer Paul L, Clark Patrick, Hughes Stephen H, Janssen Paul A J, Arnold Eddy

Abstract excerpt

Anti-AIDS drug candidate and non-nucleoside reverse transcriptase inhibitor (NNRTI) TMC125-R165335 (etravirine) caused an initial drop in viral load similar to that observed with a five-drug combination in naïve patients and retains potency in patients infected with NNRTI-resistant HIV-1 variants. TMC125-R165335 and related anti-AIDS drug candidates can bind the enzyme RT in multiple conformations and thereby...

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PMID: 15115397
DOI: 10.1021/jm030558s

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