Biomedical subjects

Satya P Gupta

Publications and source records attributed to Satya P Gupta.

4 recordsLinked to original sources

PubMed2003

Quantitative structure-activity relationships of carbonic anhydrase inhibitors.

A review is presented of quantitative structure-activity relationships (QSARs) of different categories of carbonic anhydrase (CA) inhibitors, which are basically benzenesulfonamides, heterocyclic sulfonamides and aliphatic sulfonamides. The review shows that in all categories, the inhibition potency depends largely on the electronic properties of the sulfonamide group, which can be affected by the electronic characteristics of the substituents present on the nucleus (benzene or heterocyclic ring) of the sulfonamide molecules. Substituents themselves can be involved, along with the nucleus, in some dispersion interaction with the enzyme. Based on this review, a schematic model is presented to represent the interaction of sulfonamides with the CA.

Animals↗

PubMed2003

Quantitative structure-activity relationships of renin inhibitors.

A review is presented on quantitative structure-activity relationships (QSARs) of renin inhibitors which have potential as antihypertensive and cardiovascular agents. They inhibit the renin, an enzyme that is involved in the rate-limiting first step of the renin angiotensin system (RAS). Most of the renin inhibitors are peptidomimetics but recently some nonpeptidomimetic renin inhibitors with low molecular weight have also been developed. In both types of renin inhibitors, the QSARs have exhibited that their inhibition activity would largely depend upon the molecular weight of the compounds, van der waals radius related parameters of the substituents, and the localized electronic effects, particularly of the side chain of the residues substituted in the peptides.

Algorithms↗

PubMed2002

Advances in QSAR studies of HIV-1 reverse transcriptase inhibitors.

A review is presented of the recent advances in quantitative structure-activity relationship (QSAR) studies of HIV-1 reverse transcriptase (RT) inhibitors. These inhibitors have been put into two classes: nucleoside RT inhibitors (NRTIs), which are 2',3'-dideoxynucleoside analogues (ddNs), and non-nucleoside RT inhibitors (NNRTIs). For NRTIs (ddNs), which act as competitive inhibitors or alternate substrates of RT and hence interact at the substrate binding site of the enzyme, QSARs have pointed out the major role of the electronic factors governing their activity. For NNRTIs, which bind to a site entirely distinct from the substrate binding site, the activity has been shown to be largely dependent upon the hydrophobic nature of the compounds or substituents. The hydrophobic nature of the active site in the receptor with which the NNRTIs interact provides relatively few possibilities for the molecules to have polar interactions or hydrogen bondings, but QSARs have indicated that NNRTIs do involve some polar interactions and hydrogen bondings with some pockets of the enzyme. QSARs also indicate the significant roles of steric interactions and conformational shape of the molecule.

Algorithms↗

PubMed2002

Quantitative structure-activity relationship studies on cholecystokinin antagonists.

A review is presented on quantitative structure-activity relationship (QSAR) studies on cholecystokinin antagonists. Cholecystokinin (CCK) is a gastrointestinal peptide hormone closely related chemically to gastrin. However, its receptors are found in both peripheral and central nervous systems. Those present in peripheral system have been termed as CCK-A receptors and those present in central nervous system as CCK-B receptors. QSAR studies verify that CCK-B receptors are closely related structurally to gastrin receptors. QSAR studies have been reported on different classes of CCK antagonists, e.g., benzodiazepine derivatives, amino acid derivatives, quinazolinones, and peptides and pseudopeptide analogs. These QSAR studies unravel the mechanisms of interactions of each category of antagonists with the CCK receptors. In the case of benzodiazepines, the hydrophobic interactions and hydrogen bondings are found to be the most important binding force, while in the case of quinazolinones, only the hydrogen bonding is found to be important. The hydrophobic as well as the dispersion interactions are shown to be important for the binding of glutamic acid analogs and steric factors appear to govern the activity of peptides and pseudopeptide analogs.

Amino Acid Sequence↗