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Effect of molecular size on carbonic anhydrase inhibition by sulfonamides
Author(s) -
Kumar Kamal,
Bindal Mahesh C.,
Singh Prithvi,
Gupta Satya P.
Publication year - 1981
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560200112
Subject(s) - chemistry , van der waals force , sulfonamide , carbonic anhydrase , substituent , carbonic anhydrase ii , enzyme , enzyme inhibition , stereochemistry , active site , van der waals radius , binding site , computational chemistry , organic chemistry , biochemistry , molecule
The molecular size is found to play an important role in carbonic anhydrase (CA) inhibition by sulfonamides. Significant correlation is obtained between the inhibitory power of meta ‐substituted analogs and the van der Waals volume ( V w ) of the substitutents. This provides a theoretical basis to map the active sites in enzyme and find the nature of sulfonamide‐receptor binding. It is inferred that in addition to well known binding of sulfamyl group with Zn 2+ ion of the enzyme, the meta substituent of sulfonamides interacts with some secondary binding site and this interaction is argued to be of van der Waals type.