Alcohol-induced retarded protein dynamics of human serum albumin unveiled by temperature jump

被引：0

作者：

Kao, Tzu-Lan ^{[1
]}

Chu, Li-Kang ^{[1
]}

机构：

[1] Natl Tsing Hua Univ, Dept Chem, 101,Sec 2,Kuang Fu Rd, Hsinchu 300044, Taiwan

来源：

CHEMICAL PHYSICS LETTERS | 2023年 / 833卷

关键词：

human serum albumin (HSA); Temperature jump; Protein dynamics; Blood alcohol concentration; TRYPTOPHAN FLUORESCENCE-SPECTRA; ETHANOL OR/AND CAPTOPRIL; LOG-NORMAL COMPONENTS; DRUG BINDING-SITES; CIRCULAR-DICHROISM; DENATURATION; DECOMPOSITION; REGION; GNHCL;

D O I：

10.1016/j.cplett.2023.140899

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The addition of ethanol at concentrations <= 1.0 vol% in human serum albumin (HSA) at the physiological concentration (ca. 47 mg L-1) does not influence the secondary structure but decelerates the protein dynamic process of HSA upon thermal stimulus probed by fluorescent temperature jump technique. The biological implication may be that inebriated persons are less sensitive to environmental stimuli because their HSA molecules may act more slowly when interacting with chemicals in the blood. This result provides an alternative perspective on the role of alcohol in perturbing the biological function of HSA at the molecular level.

引用

页数：6

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