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Scripps Research scientists find two compounds that lay the foundation for a new class of AIDS drug
Date:2/3/2010

sis developed from computational modeling that HIV protease has pockets on its surface besides the active site that can bind drugs. Drugs developed to target these sites could be used to make current FDA-approved active site inhibitors more potent and to restore their effectiveness against drug-resistant superbugs. The whole strategy of targeting non-active sites may also prove useful against other diseases, especially when there are mutations that cause drug resistance."

The Long Arms of HIV Protease

Approximately 33 million people are currently living with HIV infections, 2.7 million of whom were newly infected in 2008, according to the most recent statistics available from the World Health Organization. While HAART therapy has prolonged survival and improved the quality of life for many AIDS patients, a rapidly growing portion of new HIV infections involve drug-resistant strains.

Perryman has been interested in the problem of drug resistance for some time. As a Howard Hughes Medical Institute (HHMI) pre-doctoral fellow in the laboratory of HHMI Professor J. Andrew McCammon at the University of California, San Diego, Perryman conducted extensive computer simulations of a drug-resistant HIV protease molecule and compared them with a normal HIV protease molecule. This theoretical effort laid the groundwork for the current experimental study.

As is often the case in biology, the shape of the HIV protease reflects and dictates its function. In the process of reproducing itself, the virus makes long protein chains, which the protease splits into shorter pieces to enable the final assembly of new HIV virions. To split off the pieces from the longer chain, the protease has two scissor-like flaps on each side of the molecule. The flaps open to let in the viral protein chain, which threads itself into the active site binding pocket. The flaps then close, crossing in the middle over a binding pocket and cleaving the protein chain into s
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Contact: Keith McKeown
kmckeown@scripps.edu
858-784-8134
Scripps Research Institute
Source:Eurekalert

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