1Bharti Vidyapeeth's College of Pharmacy, Near Chitranagari, Kolhapur-414 003, Maharashtra, India
2New Arts, Commerce and Science College, Near Lal Taki, Ahmednagar-414 111, Maharashtra, India
P.D.V.V.P.F's College of Pharmacy, Vilad Ghat, Post MIDC, Ahmednagar-414 111, Maharashtra, India
*For correspondence-sawantrl@yahoo.com
Protease cuts the long chain of viral proteins produced by the host cell for assembly into a new functional virus. Retroviral proteases has been identified as potential targets for structurebase drug design as its inactivation leads to the production of immature, noninfectious viral particles. Structure assisted drug developments of retroviral protease inhibitors have been resulted into ten drugs approved and others are undergoing clinical trials. High-resolution structures are now available for enzymes from human immunodeficiency virus type 1 and 2, simian immunodeficiency virus, feline immunodeficiency virus, rous sarcoma virus and equine infectious anemic virus. This review summarizes the data documenting location, structures, functions and inhibition of retroviral proteases. Structure of target enzyme, binding of inhibitors to the target enzyme and common structural features of existing inhibitors could be useful for development of novel compounds with even more pertinent pharmacological and pharmacokinetic profile.
Retroviral proteases (RPs), structure, function, protease inhibitors (PIs)