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S Sowmya

Publications and source records attributed to S Sowmya.

5 recordsLinked to original sources
PubMed1998

A quantitative structure-activity relationship study on some sulfolanes and arylthiomethanes acting as HIV-1 protease inhibitors.

A quantitative structure-activity relationship (QSAR) study on some sulfolanes and arylthiomethanes acting as human immunodeficiency virus-1 (HIV-1) protease inhibitors reveals that in the case of sulfolanes an octahydropyrindene ring and a five-membered 3(S)-sulfolane ring with a hydrophobic 2-substituent (cis to 3-substituent) will be crucial for the inhibition activity. The binding of a sulfolane, which is a nonpeptidic molecule, with the enzyme is shown to partly mimic the binding of a peptidic inhibitor. The 2-substituent is found to have strong hydrophobic interaction with the receptor. Similarly, in the case of arylthiomethanes, one of the substituents of the methane is found to have strong hydrophobic interaction with the enzyme, while the aryl substituent (4-hydroxy-6-phenyl-2-oxo-2H-pyran-3-yl) is assumed to be involved in the hydrogen bondings.

Crystallography, X-Ray↗
PubMed1998

Quantitative structure-activity relationship studies on cyclic urea-based HIV protease inhibitors.

A quantitative structure-activity relationship (QSAR) study is described on some cyclic ureas that inhibit the enzyme HIV-1 protease (HIV-1-PR) and exhibit antiviral potency. Both the enzyme inhibition activity and the antiviral potency were found to be primarily governed by the hydrophobic property of the substituents at the nitrogens (N2/N2') of the urea. Adjacent to the nitrogens, the C1/C1'-substituents are, however, found to affect the activity (inhibition) by their molecular size. The essential binding of the ureas with the receptor is, however, through multiple hydrogen bonding, where the substituents, too, can participate in such binding if they are capable of doing so. A schematic diagram of the overall interaction of the inhibitors with the receptor is presented.

HIV Protease Inhibitors↗