Determination of drug binding sites to proteins by electrospray ionisation mass spectrometry: the interaction of cisplatin with transferrin

被引：88

作者：

Allardyce, CS

Dyson, PJ ^{[1
]}

Coffey, J

Johnson, N

机构：

[1] Ecole Polytech Fed Lausanne, Inst Chim Minerale & Analyt, BCH, CH-1015 Lausanne, Switzerland

[2] Micromass UK Ltd, Manchester M22 5PP, Lancs, England

来源：

RAPID COMMUNICATIONS IN MASS SPECTROMETRY | 2002年 / 16卷 / 10期

关键词：

D O I：

10.1002/rcm.662

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Cisplatin, CiS-[PtCl2(NH3)(2)], is known to bind to human serum transferrin, but the binding site remains a matter of some debate. Electrospray ionisation mass spectrometry has been used to characterise the interaction of cisplatin with transferrin. The studies indicate that cisplatin initially docks with, and subsequently bonds covalently to, the hydroxyl functional group of threonine 457, with the loss of HCl affording a transferrin-O-PtCl(NH3)(2) adduct. Copyright (C) 2002 John Wiley Sons, Ltd.

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页码：933 / 935

页数：3

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