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Proteochemometrics achieves better retardants for HIV/Aids

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09.03.2007

A new method for analysis of retroviral proteins gives new opportunities to the development of novel retardants for HIV/Aids. The study, which was published in the March issue of PLoS Computational Biology, shows how to in a very exact way analyze the interaction of drug targets with small molecules.

 

The new method, developed by Professor Jarl Wikberg at Uppsala University, allowed the researchers to create a ‘map’ that in detail shows how 61 drug targets from nine different retroviruses interact with surrounding molecules.


The problem in HIV is that the virus mutates very easily. This leads to appearance of new strains that escape the body’s immune defence as well as drug retardants. The virus becomes resistant to the retardant and the treatment fails.

“This is a large problem. Resistant strains appear gradually in all patients irrespectively which combinations of the present treatments are used. Finally there is no alternative to treat the patient”, says Jarl Wikberg.

The new method – proteochemometrics – makes it possible to predict how effectively drug candidates will retard different HIV-strains. This makes it a relatively simple matter to design new drugs that concomitantly retards many different resistance strains of HIV.

“We predict that it will be substantially more difficult for the virus to escape a retardant that has been designed with use of proteochemometrics compared to the presently used retardants”, says Jarl Wikberg, and continues:

“The pharmaceutical industry has already shown a great interest to our approach and we have great hopes that it, within a relatively short time span, will result in new improved retardants for treatment of HIV/Aids”.

The article, published in PLoS Computational Biology, can be read at: http://dx.doi.org/10.1371/journal.pcbi.0030048

For more information contact Jarl Wikberg, phone: +46 (0)18-471 42 38; cell phone: +46 (0)70-3 449 549; e-mail: Jarl.Wikberg@farmbio.uu.se

Anneli Waara | Source: alphagalileo
Further information: dx.doi.org/10.1371/journal.pcbi.0030048
www.uu.se

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