Download MendeleyImproved cyclic urea inhibitors of the HIV-1 protease: synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450.
Hodge, C.N., Aldrich, P.E., Bacheler, L.T., Chang, C.H., Eyermann, C.J., Garber, S., Grubb, M., Jackson, D.A., Jadhav, P.K., Korant, B., Lam, P.Y., Maurin, M.B., Meek, J.L., Otto, M.J., Rayner, M.M., Reid, C., Sharpe, T.R., Shum, L., Winslow, D.L., Erickson-Viitanen, S.(1996) Chem Biol 3: 301-314
- PubMed: 8807858
- DOI: https://doi.org/10.1016/s1074-5521(96)90110-6
- Primary Citation of Related Structures:
1DMP - PubMed Abstract:
Effective HIV protease inhibitors must combine potency towards wild-type and mutant variants of HIV with oral bioavailability such that drug levels in relevant tissues continuously exceed that required for inhibition of virus replication. Computer-aided design led to the discovery of cyclic urea inhibitors of the HIV protease. We set out to improve the physical properties and oral bioavailability of these compounds.
Organizational Affiliation:
Department of Chemical Sciences, DuPont Merck Pharmaceutical Co., Wilmington, DE 19880, USA. hodgecn@carbon.dmpc.com
