Molecular insights into complexation between protein and silica: Spectroscopic and simulation investigations

•Complexation of proteins and silica caused severe membrane fouling.•Silica induced the unfolding of proteins in different extents.•Proteins promoted the polymerization of silica.•Calcium ions functioned as “bridges” in the complexation of silica and proteins.•Molecular docking and DFT calculations...

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Published in:Water research (Oxford) 2023-11, Vol.246, p.120681-120681, Article 120681
Main Authors: Jiang, Ting, Hu, Xiao-Fan, Guan, Yan-Fang, Chen, Jie-Jie, Yu, Han-Qing
Format: Article
Language:English
Subjects:
In situ spectroscopy
Protein unfolding
Protein-silica complexation
Silica polymerization
Simulations
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Summary:•Complexation of proteins and silica caused severe membrane fouling.•Silica induced the unfolding of proteins in different extents.•Proteins promoted the polymerization of silica.•Calcium ions functioned as “bridges” in the complexation of silica and proteins.•Molecular docking and DFT calculations revealed the binding sites. The synergistic effect of protein-silica complexation leads to exacerbated membrane fouling in the membrane desalination process, exceeding the individual impacts of silica scaling or protein fouling. However, the molecular-level dynamics of silica binding to proteins and the resulting structural changes in both proteins and silica remain poorly understood. This study investigates the complexation process between silica and proteins—negatively charged bovine serum albumin (BSA) and positively charged lysozyme (LYZ) at neutral pH—using infrared spectroscopy (IR), in situ attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), and multiple computational simulations. The findings reveal that both protein and silica structures undergo changes during the complexation process, with calcium ions in the solution significantly exacerbating these alterations. In particular, in situ ATR-FTIR combined with two-dimensional correlation spectroscopy analysis shows that BSA experiences more pronounced unfolding, providing additional binding sites for silica adsorption compared to LYZ. The adsorbed proteins promote silica polymerization from lower-polymerized to higher-polymerized species. Furthermore, molecular dynamics simulations demonstrate greater conformational variation in BSA through root-mean-square-deviation analysis and the bridging role of calcium ions via mean square displacement analysis. Molecular docking and density functional theory calculations identify the binding sites and energy of silica on proteins. In summary, this research offers a comprehensive understanding of the protein-silica complexation process, contributing to the knowledge of synergistic behaviors of inorganic scaling and organic fouling on membrane surfaces. The integrated approach used here may also be applicable for exploring other complex complexation processes in various environments.
ISSN:0043-1354
1879-2448
DOI:10.1016/j.watres.2023.120681