Effect of molecular size on carbonic anhydrase inhibition by sulfonamides
✍ Scribed by Kamal Kumar; Mahesh C. Bindal; Prithvi Singh; Satya P. Gupta
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 310 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0020-7608
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✦ Synopsis
Abstract
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.
📜 SIMILAR VOLUMES
Pore size control of a series of activated carbon fibers was attempted by chemical vapor deposition (CVD) of benzene to clarify the influence of the pore distribution on the development of molecular sieving ability. Weight increase by CVD was found to saturate at a certain level respective to the fi