title: Exploring structural requirements for aldose-reductase inhibition by 2,4-dioxo-5-(naphth-2-ylmethylene)-3-thiazolidinyl acetic acids and 2-thioxo analogues: Fujita-Ban and Hansch approach.
abstract: A Quantitative Structure-Activity Relationship (QSAR) study based on Fujita-Ban and classical Hansch approach was performed on 2,4-dioxo-5-(naphth-2-ylmethylene)-3-thiazolidinyl acetic acids and 2-thioxo analogues to gain structural insight into the binding mode of the molecules to the aldose-reductase enzyme. First, the Fujita-Ban approach has been followed, which revealed the highest activity contribution for 2-thioxo analogues of 3-thiazolidinyl acetic acids as compared to 2,4-dioxo analogues. Further, the Hansch approach confirms that 2-thioxo-4-oxo-3-thiazolidinyl acetic acids are conducive to aldose-reductase inhibitory activity. The hydrophobic properties of the various substituents have been found to play major roles in the binding of these compounds with the receptor.
authors.affiliation: CADD Laboratory, Department of Pharmacy, Shri G. S. Institute of Technology & Science, Indore, India. lovesoni@hotmail.com
authors.forename: Love Kumar
authors.initials: LK
authors.lastname: Soni
authors.forename: Satish G
authors.initials: SG
authors.lastname: Kaskhedikar
mesh_terms: D000085:Acetates / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D000449:Aldehyde Reductase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D008961:Models, Structural; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D021281:Quantitative Structure-Activity Relationship; D013844:Thiazoles / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology
chemical_list: D000085:Acetates; D004791:Enzyme Inhibitors; D013844:Thiazoles; D000449:Aldehyde Reductase