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Synthesis and carbonic anhydrase inhibitory effects of novel sulfamides derived from 1-aminoindanes and anilines.

Authors
  • Akbaba, Yusuf
  • Bastem, Enes
  • Topal, Fevzi
  • Gülçin, Ilhami
  • Maraş, Ahmet
  • Göksu, Süleyman
Type
Published Article
Journal
Archiv der Pharmazie
Publisher
Wiley (John Wiley & Sons)
Publication Date
Dec 01, 2014
Volume
347
Issue
12
Pages
950–957
Identifiers
DOI: 10.1002/ardp.201400257
PMID: 25223956
Source
Medline
Keywords
License
Unknown

Abstract

Three 1-aminoindanes, four anilines and BnOH or t-BuOH were reacted with chlorosulfonyl isocyanate to give sulfamoyl carbamates. Pd-C catalysed hydrogenolysis reactions of carbamates or deprotection of the Boc group of the carbamates with CF3 CO2 H afforded seven novel sulfamides. Human carbonic anhydrase (hCA) isoenzymes I and II (hCA I and hCA II) were purified from fresh human blood erythrocytes with one-step affinity chromatography on Sepharose 4B-tyrosine-sulfanilamide. The inhibitory properties of the novel sulfamides on both isoenzymes were determined using the esterase activity with 4-nitrophenyl acetate (NPA) as substrate. The tested novel sulfamides derived from 1-aminoindanes and anilines effectively inhibited hCA I and II competitively in the nanomolar range. Among these compounds, the novel sulfamide derivative 17 showed the most potent inhibitory effect against hCA I (Ki : 153.88 nM), while sulfamide derivative 26 showed the highest inhibitory potential against hCA II (Ki : 117.80 nM).

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