Binding modes of two highly potent and nontoxic inhibitors of HIV-1 integrase.
Conf Proc IEEE Eng Med Biol Soc
; 2004: 3003-6, 2004.
Article
en En
| MEDLINE
| ID: mdl-17270910
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Conf Proc IEEE Eng Med Biol Soc
Asunto de la revista:
ENGENHARIA BIOMEDICA
Año:
2004
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Estados Unidos