Premium
Schiff bases and their amines: Synthesis and discovery of carbonic anhydrase and acetylcholinesterase enzymes inhibitors
Author(s) -
Yiğit Beyhan,
Yiğit Murat,
Taslimi Parham,
Gök Yetkin,
Gülçin İlhami
Publication year - 2018
Publication title -
archiv der pharmazie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 61
eISSN - 1521-4184
pISSN - 0365-6233
DOI - 10.1002/ardp.201800146
Subject(s) - chemistry , carbonic anhydrase , acetylcholinesterase , sodium borohydride , stereochemistry , enzyme , carbonic anhydrase i , schiff base , proton nmr , active site , amine gas treating , medicinal chemistry , organic chemistry , catalysis
Three series of symmetrical Schiff bases were synthesized from 1,2‐diaminoethane, 1,3‐diaminopropane and 1,4‐diaminobutane and substituted benzaldehydes, and reduced by sodium borohydride to the corresponding benzylic diamines 4–6 . All of the compounds obtained were characterized using elemental analysis, FT‐IR, 1 H NMR, and 13 C NMR spectroscopy. The enzyme inhibitory properties of these compounds were tested and the influence of the alkane chain length and the substituents on the phenyl group on the enzyme inhibition activity were examined. The novel Schiff bases and their amine derivatives ( 1a–d , 2a–d , 3b–d , 4a–c , 5a–c , 6a , 6c , 6d ) were effective inhibitors of the cytosolic carbonic anhydrase I and II isoforms (hCA I and II), and acetylcholinesterase (AChE) with K i values in the range of 159.43 ± 30.03 to 563.73 ± 115.30 nM for hCA I, 104.88 ± 18.44 to 524.32 ± 95.03 nM for hCA II, and 3.95 ± 0.74 to 30.83 ± 6.81 nM for AChE.