alexa Binding modes of two highly potent and nontoxic inhibitors of HIV-1 integrase.
Infectious Diseases

Infectious Diseases

Journal of AIDS & Clinical Research

Author(s): Zhu HM, Chen WZ, Wang CX, Zhu HM, Chen WZ, Wang CX

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Abstract The complex structures of Human Immunodeficiency Virus Type 1 (HIV-1) integrase binding two highly potent and nontoxic inhibitors, lithospermic acid (M/sub 5/22) and lithospermic acid B (M/sub 5/32), were obtained using docking calculations. Docking results provided detailed information of their binding modes. The binding sites of M/sub 5/22 and M/sub 5/32 were similar to the inhibitor 5-CITEP. The lowest docking energies for HIV-1 integrase binding M/sub 5/22 and M/sub 5/32 are in agreement with their corresponding lower IC/sub 50/ values. Our results on the chemical structure difference between M/sub 5/22 and M/sub 5/32 show that the carboxyl and hydroxyl groups on the side-chain of M/sub 5/32 are important chemical groups which could help to increase the effect against HIV-1 IN replication. This article was published in Conf Proc IEEE Eng Med Biol Soc and referenced in Journal of AIDS & Clinical Research

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