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Summer Research Fellowship Programme of India's Science Academies

Crystallographic and Biophysical Studies on HIV-1 Protease-Inhibitor Complexes

Dr. Pranita Bhatele

Department of Biotechnology, MataGujri Mahila Mahavidyalaya, Jabalpur, M.P. 482001

Dr Mukesh Kumar

Dr. Vishal Parashar, Radiation Biology and Health Science Division, Bhabha Atomic Research Center, Mumbai

Abstract

Human Immunodeficiency Virus (HIV) is a complex retrovirus which has proved fatal over the years taking millions of lives. Protease is one of the 3 enzymes present in HIV and is required for proper maturation of the virus. The virus makes long polypeptide chain that contains many proteins during replication. This precursor polyprotein must be cleaved at 9 specific sites without which the virus cannot produce mature copies of itself. Since it is an essential component of the viral life cycle, HIV-1 protease is an important target for design of inhibitors. In this project Recombinant HIV-1 protease was expressed and purified from inclusion bodies. The refolded protein was characterized using circular dichroism spectropolarimetry. The purity of protein was judged from SDS PAGE. Purified protein was crystallized with and without an inhibitor. Isothermal titration calorimetry was carried out to determine the binding parameters of acetyl pepstatin with HIV-1 protease. X-ray diffraction data will be collected on these crystals to know the mode of binding of the inhibitor.

Keywords: Human Immuno deficiency virus, AIDS, Protease, Crystal, X-ray crystaloography

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