IIT Madras researchers find ways to develop more effective drugs to treat HIV/AIDS

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IIT Madras researchers are working in the direction of targeting HIV-1 protease.Researchers at the Indian Institute of Technology Madras are working on a revolutionary idea that can help develop effective drugs for the treatment of HIV/AIDS. The team of researchers said that the efficacy of drugs against the HIV virus can be enhanced by introducing electrostatic interaction sites on molecules of the potential drug. The findings of the research – led by Prof. Sanjib Senapati, Department of Biotechnology, IIT Madras along with research scholars Chinmai Pindi and Mohammed Ahsan – have been published in Biochemistry, a peer-review Journal of the American Chemical Society.

AIDS is a major cause of death in several countries and researchers have been working to find an effective drug for the disease since its outbreak nearly four decades ago. In a bid to find better drugs to combat HIG strains, researchers of IITM decided to explore more about the molecular structure of the protease to figure out weak sites that can offer better understanding for enhanced inhibitor development.

Researchers are working in the direction of targeting HIV-1 protease. AIDS virus uses this essential enzyme for maturation and growth. Drug developers are aiming at developing efficient inhibitors of the enzyme. Inhibitors make enzymes unavailable to the virus by binding with them.

Elaborating it, Professor Senapati said, “Currently, inhibitors use weak forces of attraction to target HIVPR. This force is called ‘van der Waal’s forces’ and is used to attach themselves to the protease molecule. Because of the weak force, the virus soon becomes resistant to the drug.”

Professor Senapati and his team have used state-of-art computational techniques to uncover vital data that will be useful in developing more efficacious drugs. IIT Madras researchers conducted Molecular Dynamics (MD) simulation studies and found that if a drug molecule can be designed with a complementary charge, it can permanently inhibit/deactivate the enzyme.

“There is no electrostatic complementarity in drugs currently available. It is well known that electrostatic forces between molecules are far more strong than van der Waals forces and therefore it is important to investigate it,” the professor said.

The researchers have proposed that both electrostatic and van der Waals interactions should be embraced to complement the HIVPR active site architecture.

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