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Discovery of MK-8718, an HIV Protease Inhibitor Containing a Novel Morpholine Aspartate Binding Group

2016; American Chemical Society; Volume: 7; Issue: 7 Linguagem: Inglês

10.1021/acsmedchemlett.6b00135

1948-5875

Christopher J. Bungard, Peter Williams, Jeanine Ballard, David Jonathan Bennett, Christian Beaulieu, Carolyn Bahnck-Teets, Steve S. Carroll, Ronald K. Chang, David C. Dubost, John F. Fay, Tracy L. Diamond, Thomas J. Greshock, Hao Li, M. Katharine Holloway, Peter J. Felock, Jennifer J. Gesell, Hua-Poo Su, Jesse J. Manikowski, Daniel J. McKay, Mike Miller, Xu Min, Carmela Molinaro, Oscar Moradei, Philippe G. Nantermet, Christian Nadeau, Rosa I. Sánchez, Tummanapalli Satyanarayana, William D. Shipe, Sanjay K. Singh, Vouy Linh Truong, S. Vijayasaradhi, Catherine M. Wiscount, Joseph P. Vacca, Sheldon N. Crane, John A. McCauley,

HIV Research and Treatment

A novel HIV protease inhibitor was designed using a morpholine core as the aspartate binding group. Analysis of the crystal structure of the initial lead bound to HIV protease enabled optimization of enzyme potency and antiviral activity. This afforded a series of potent orally bioavailable inhibitors of which MK-8718 was identified as a compound with a favorable overall profile.