Ethanol or/and captopril-induced precipitation and secondary conformational changes of human serum albumin

被引：58

作者：

Lin, SY ^{[1
]}

Li, MJ ^{[1
]}

Wei, YS ^{[1
]}

机构：

[1] Vet Gen Hosp Taipei, Dept Med Res & Educ, Biopharmaceut Lab, Taipei, Taiwan

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 2004年 / 60卷 / 13期

关键词：

captopril; ethanol; HSA; precipitation; Fr-IR/DSC; secondary structure; transformation;

D O I：

10.1016/j.saa.2004.03.001

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

We determined the secondary structure of solid-state native human serum albumin (HSA) and its precipitates induced by ethanol, captopril, or a captopril/ethanol mixture. A transmission Fourier transform infrared (FT-IR) microspectroscopy equipped with a thermal analyzer was used. The secondary structural composition of solid-state native HSA was 54% alpha-helices (1655 cm(-1)), 22% beta-turns (1679 cm(-1)), and 23% beta-sheets (1633 cm(-1)). After ethanol treatment, a new peak was observed at 1690cm(-1), and the peak at 1633 cm(-1) was more apparent in the HSA precipitates. The corresponding compositions consisted of 59% alpha-helices, 17% beta-turns, and 24% beta-sheets. After treatment with captopril with or without ethanol, the percentage of alpha-helices and beta-turns decreased in both HSA precipitates, but the percentage of beta-sheets increased. The temperature-dependent structural transformation from alpha-helices/random coils to beta-sheets for the solid-state HSA samples occurred at markedly different onset temperatures. The onset temperature for native HSA was 85 degreesC, and that for HSA precipitates obtained from ethanol, captopril, or captopril/ethanol was 100, 48 or 57 degreesC, respectively. The thermal-induced structural transformation from a-helices/random coils to beta-sheets implies a partial unfolding structure in these HSA samples. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：3107 / 3111

页数：5

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