PROTEIN-BINDING INVESTIGATION BY DIFFERENCE CIRCULAR-DICHROISM - NATIVE AND ACETYLATED HUMAN SERUM ALBUMINS

被引：16

作者：

BERTUCCI, C ^{[1
]}

VIEGI, A ^{[1
]}

ASCOLI, G ^{[1
]}

SALVADORI, P ^{[1
]}

机构：

[1] UNIV PISA,CNR,CTR STUDIO MACROMOLEC STEREORDINATE & OTTICAMENTE,DIPARTIMENTO CHIM & CHIM IND,I-56126 PISA,ITALY

来源：

CHIRALITY | 1995年 / 7卷 / 02期

关键词：

PROTEIN BINDING; CIRCULAR DICHROISM; HUMAN SERUM ALBUMIN; STEREOSELECTIVITY; DRUGS; MODIFIED ALBUMIN;

D O I：

10.1002/chir.530070202

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

A modified albumin was prepared by selective reaction of Lys(199) with acetyl salicylic acid. Protein binding investigation was carried out on native and modified proteins by difference circular dichroism (Delta CD). Acetylation of Lys(199) reduces significantly the effects of the interaction between drugs in the stereoselective HSA binding at specific binding areas. (C) 1995 Wiley-Liss, Inc.

引用

页码：57 / 61

页数：5

共 43 条

[1] STEREOCHEMICAL FEATURES OF 1,4-BENZODIAZEPIN-2-ONES BOUND TO HUMAN SERUM-ALBUMIN - DIFFERENCE CD AND UV STUDIES [J].