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. 2002 Jan 23;16(1):84–87. doi: 10.1002/ptr.969

Quaternary benzo[c]phenanthridine alkaloids as inhibitors of aminopeptidase N and dipeptidyl peptidase IV

Aleksi Šedo 1, Květoslava Vlašicová 1, Petr Barták 2, Radim Vespalec 3, Jaroslav Vičar 4, Vilim Šimánek 4, Jitka Ulrichová 4,
PMCID: PMC7168101  PMID: 11807974

Abstract

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 μm, 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 μm) 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.

Keywords: benzo[c]phenanthridines, Macleaya cordata, C6 rat glioma cells, aminopeptidase N, dipeptidyl peptidase IV, albumin, binding constants

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