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Environmental problems - Chemical approaches
RESEARCH ARTICLE

Binding mechanism of single-walled carbon nanotubes (SWCNTs) to serum albumin: spectroscopy and molecular modelling exploration

Ying Hai A , Kaili Qu A , Yaquan Liu A and Chunyan Zhao orcid.org/0000-0003-4163-1848 A B
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A School of Pharmacy, Lanzhou University, Lanzhou, 730000, China.

B Corresponding author. Email: zhaochy07@lzu.edu.cn

Environmental Chemistry 15(5) 278-285 https://doi.org/10.1071/EN18043
Submitted: 22 February 2018  Accepted: 21 April 2018   Published: 1 August 2018

Environmental context. Single-walled carbon nanotubes can have adverse physiological effects by interacting with proteins. Using serum bovine albumin as a model protein, we investigate the conformational changes in proteins at the tertiary structure level upon interaction with carbon nanotubes. This specific study of a model protein helps our understanding of the general binding mechanisms involved, and allows us to predict the potential adverse effects of carbon nanotubes interacting with other proteins.

Abstract. 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.

Additional keywords: bovine serum albumin (BSA), distribution, subdomain IB.


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