期刊
ENVIRONMENTAL CHEMISTRY
卷 15, 期 5, 页码 278-285出版社
CSIRO PUBLISHING
DOI: 10.1071/EN18043
关键词
bovine serum albumin (BSA); distribution; subdomain IB
资金
- National Natural Science Foundation of China [31000017, 21207056]
- State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences [KF2015-17]
- Key Laboratory of Chemistry and Quality for Traditional Chinese Medicines of the University of Gansu Province, Gansu University of Chinese Medicines [zzy-2016-01]
- Fundamental Research Funds for the Central Universities [lzujbky-2017-200, lzujbky-2017-kb05, LZU-JZH1914]
- Gansu Provincial Administration of Traditional Chinese Medicine [GZK-2017-63]
- Lanzhou Talent Innovation and Entrepreneurship Technology Program [2016-RC-19]
Considering the large-scale production of diversified nanomaterials, it is of paramount importance to unravel the structural details of interactions between nanoparticles and biological systems at the molecular level, with the aim to reveal the potential adverse biological impacts. Herein, with single-walled carbon nanotubes (SWCNTs) acting as model nanomaterials and bovine serum albumin (BSA) acting as a model protein, a combination of spectroscopy experiments and molecular modelling was applied to help us unravel some important issues on the mechanism of protein interactions with SWCNTs. As a result, SWCNTs were first proved to bind at subdomain IB of BSA based on fluorescence experiments and molecular dynamics modelling. In addition, hydrophobic interactions were recognised as the driving force governing the binding behaviour between the SWCNTs and BSA. As a consequence, SWCNT binding led to a conformational change both at the secondary and tertiary structure levels. Insight into the binding details between BSA and SWCNT can help understand the recognition mechanism between SWCNTs and proteins, thus be helpful to predict the potential adverse effects of SWCNTs.
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