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A possible new way to block HIV infection of healthy cells discovered

and receptor-bindings are very specific, just like putting your left hand in your left pants pocket.

Not only were the D-peptides still recognized, they fit into the receptor more snugly than their natural L-peptide counterparts, blocking the virus from bonding. Subsequent experiments, documented in the paper, showed the synthetic D-peptides have a longer half life, making them less susceptible to biological decay than L-peptides.

In making the discovery, Huang designed and synthesized the D-peptide and tested its bonding to the receptor at Illinois. Testing against HIV-1 was done at Dana-Farber in Dr. Joseph Sodroskis laboratory and by a group led by Hideko Kaji at Jefferson Medical College, where Huang had previously worked and had begun his research.

Traditional drug therapies have targeted protease or reverse transcriptase activity that occur after HIV has entered healthy cells. None stop HIV from docking with cells.

Researchers realize that this approach is not enough, Huang said. It would be nice to have other targets. Our discovery suggests the possibility of a whole new therapeutic weapon, which alone or in combination with existing therapies could work better to block AIDS.


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Contact: Jim Barlow
b-james3@uiuc.edu
217-333-5802
University of Illinois at Urbana-Champaign
15-May-2002


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