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Quaternary benzo[c]phenanthridine alkaloids as inhibitors of aminopeptidase N and dipeptidyl peptidase IV
Author(s) -
Šedo Aleksi,
Vlašicová Květoslava,
Barták Petr,
Vespalec Radim,
Vičar Jaroslav,
Šimánek Vilim,
Ulrichová Jitka
Publication year - 2002
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.969
Subject(s) - sanguinarine , chelerythrine , phenanthridine , chemistry , alkaloid , dipeptidyl peptidase , aminopeptidase , biochemistry , dipeptidyl peptidase 4 , proteases , protopine , stereochemistry , enzyme , biology , protein kinase c , leucine , amino acid , diabetes mellitus , type 2 diabetes , endocrinology
Chelerythrine, sanguinarine and an alkaloid extract from Macleaya cordata —sanguiritrin—were found to be inhibitors of aminopeptidase A and dipeptidyl peptidase IV, while fagaronine inhibited dipeptidyl peptidase IV only. At 50 μ M , chelerythrine, sanguinarine and sanguiritrin inhibited aminopeptidase N by 82%, 82%, 88%, DPP IV by 38%, 62%, 57%, and fagaronine by 34%, respectively. When bovine serum albumin (500 μg/mL) was added, the inhibition of both proteases by quaternary benzo[c]phenanthridine alkaloids (QBA) (50 μ M ) was significantly diminished. Strong interaction of chelerythrine and sanguinarine with bovine and human serum albumin was proved by electrophoretic determination of their respective conditional binding constants. Copyright © 2002 John Wiley & Sons, Ltd.