Abstract
HIV-1 integrase(IN) is one of three viral enzymes required for replication. IN mediates integration of viral DNA into the host genome in two steps: 3′-processing and strand transfer. It is currently recognized as an important target for therapeutic development against AIDS. QSAR (Quantitative Structure-Activity Relationship) modeling was utilized to study HIV-1 integrase inhibition. QSAR models were constructed to predict the IC 50 values for the two structural classes (salicyhydrazines and tyrphostins) independently and in combination. The results showed that the models for different structural classes have different dependence on the same descriptors. It suggests that salicylhydrazines and tyrphostins might have different binding sites in HIV-1 integrase.
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