期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 237, 期 -, 页码 -出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2020.118410
关键词
Binding mechanism; Acesulfame; Human serum albumin; Spectroscopy
类别
资金
- National Natural Science Foundation of China [21571154]
- Jiangsu Fundament of Qilan Project
- 333 Project
- Six Talent Peaks Project in Jiangsu Province
In this work, the binding interaction of an artificial sweetener, acesulfame (ACS) with human serum albumin (HSA) are investigated at the molecular level by using spectral methods and molecular modeling. ACS has the ability to induce static quenching of the intrinsic fluorescence of HSA by a complex formed between HSA and ACS through weak multi-noncovalent forces including hydrophobic, hydrogen bond and van der Waals forces. ACS enters subdomain IIA of HSA to induce the tertiary structure changes of HSA and decreased the hydrophobicity of protein. In addition, ACS binding does not obviously alter the secondary structure of HSA. This study is hoped to provide some crucial information for further investigations of the biosafety of sweetener. (C) 2020 Elsevier B.V. All rights reserved.
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