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The Inhibition of Bovine Kidney Hexosaminidase by N ‐Acetylglucosamine‐Related 1,2,3‐ and 1,2,4‐Triazoles Is in Agreement with an ` anti '‐Protonation
Author(s) -
Panday Narendra,
Vasella Andrea
Publication year - 2000
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/1522-2675(20000607)83:6<1205::aid-hlca1205>3.0.co;2-l
Subject(s) - chemistry , stereochemistry
The N ‐acetylglucosamine‐related 1,2,4‐triazole 14 and 1,2,3‐triazole 16 have been prepared by N ‐acetylation of the known amines 19 and 20 , and their K i values determined against bovine kidney β ‐ N ‐acetylglucosaminidase, a mammalian hexosaminidase. The 1,2,3‐triazole 16 ( K i =4 μ M ) is a markedly weaker inhibitor than the isosteric azoles 13 – 15 . The K i value of the 1,2,4‐triazole 14 (0.034 μ M ) is smaller than that of the tetrazole 13 (0.2 μ M ), but larger than that of the imidazole 15 (0.0035 μ M ), confirming the correlation between inhibitory strength and basicity of the azole, as expected on the basis of an anti ‐protonation mechanism of mammalian hexosaminidases.