Artículo
Potent inhibitors active against HIV reverse transcriptase with K101P, a mutation conferring rilpivirine resistance
Gray, William T.; Frey, Kathleen M.; Laskey, Sarah B.; Mislak, Andrea C.; Spasov, Krasimir A.; Lee, Won Gil; Bollini, Mariela
; Siliciano, Robert F.; Jorgensen, William L.; Anderson, Karen S.
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Fecha de publicación:
09/2015
Editorial:
American Chemical Society
Revista:
ACS Medicinal Chemistry Letters
e-ISSN:
1948-5875
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Catechol diether compounds have nanomolar antiviral and enzymatic activity against HIV with reverse transcriptase (RT) variants containing K101P, a mutation that confers high-level resistance to FDA-approved non-nucleoside inhibitors efavirenz and rilpivirine. Kinetic data suggests that RT (K101P) variants are as catalytically fit as wild-type and thus can potentially increase in the viral population as more antiviral regimens include efavirenz or rilpivirine. Comparison of wild-type structures and a new crystal structure of RT (K101P) in complex with a leading compound confirms that the K101P mutation is not a liability for the catechol diethers while suggesting that key interactions are lost with efavirenz and rilpivirine.
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Articulos(OCA HOUSSAY)
Articulos de OFICINA DE COORDINACION ADMINISTRATIVA HOUSSAY
Articulos de OFICINA DE COORDINACION ADMINISTRATIVA HOUSSAY
Citación
Gray, William T.; Frey, Kathleen M.; Laskey, Sarah B.; Mislak, Andrea C.; Spasov, Krasimir A.; et al.; Potent inhibitors active against HIV reverse transcriptase with K101P, a mutation conferring rilpivirine resistance; American Chemical Society; ACS Medicinal Chemistry Letters; 6; 10; 9-2015; 1075-1079
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