Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

doi:10.1016/j.cjche.2022.06.014

Chinese Journal of Chemical Engineering ›› 2022, Vol. 50 ›› Issue (10): 369-378.DOI: 10.1016/j.cjche.2022.06.014

• Biotechnology and Bioengineering • Previous Articles Next Articles

Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Qingxia Xiong^1,2, Ying Ren^1,4,5, Yufei Xia^3,4,5, Guanghui Ma^3,4,5, Reiji Noda², Wei Ge^1,2,4,5

1 State Key Laboratory of Multiphase Complex Systems, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;
2 Division of Environmental Engineering Science, Graduate School of Science and Technology, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma 376-8515, Japan;
3 State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;
4 School of Chemical Engineering, University of Chinese Academy of Sciences, Beijing 100049, China;
5 Innovation Academy for Green Manufacture, Chinese Academy of Sciences, Beijing 100190, China

Received:2022-05-18 Revised:2022-06-17 Online:2023-01-04 Published:2022-10-28
Contact: Ying Ren,E-mail:yren@ipe.ac.cn
Supported by:
This work was financially supported by the National Natural Science Foundation of China (Nos. 21821005, 21973097, 92034302 and 91834303), the Innovation Academy for Green Manufacture, Chinese Academy of Sciences (IAGM-2019-A03 and IAGM-2019-A13) and Key Research Program of Frontier Science, Chinese Academy of Sciences (QYZDJ-SSW-JSC029). We also acknowledge the computational resources provided by HPC Cluster of Mole-8.5E at Institute of Process Engineering, Chinese Academy of Sciences.

Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Qingxia Xiong^1,2, Ying Ren^1,4,5, Yufei Xia^3,4,5, Guanghui Ma^3,4,5, Reiji Noda², Wei Ge^1,2,4,5

1 State Key Laboratory of Multiphase Complex Systems, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;
2 Division of Environmental Engineering Science, Graduate School of Science and Technology, Gunma University, 1-5-1 Tenjin-cho, Kiryu, Gunma 376-8515, Japan;
3 State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China;
4 School of Chemical Engineering, University of Chinese Academy of Sciences, Beijing 100049, China;
5 Innovation Academy for Green Manufacture, Chinese Academy of Sciences, Beijing 100190, China

通讯作者: Ying Ren,E-mail:yren@ipe.ac.cn
基金资助:
This work was financially supported by the National Natural Science Foundation of China (Nos. 21821005, 21973097, 92034302 and 91834303), the Innovation Academy for Green Manufacture, Chinese Academy of Sciences (IAGM-2019-A03 and IAGM-2019-A13) and Key Research Program of Frontier Science, Chinese Academy of Sciences (QYZDJ-SSW-JSC029). We also acknowledge the computational resources provided by HPC Cluster of Mole-8.5E at Institute of Process Engineering, Chinese Academy of Sciences.

Abstract

Abstract: The adsorption of protein molecules to oil/water (O/W) interface is of critical importance for the product design in a wide range of technologies and industries such as biotechnology, food industry and pharmaceutical industry. In this work, with ovalbumin (OVA) as the model protein, the adsorption conformations at the O/W interface and the adsorption stability have been systematically studied via multiple simulation methods, including all-atom molecular dynamic (AAMD) simulations, coarse-grained molecular dynamic (CGMD) simulations and enhanced sampling methods. The computational results of AAMD and CGMD show that the hydrophobic tail of OVA tends to be folded under long time relaxation in aqueous phase, and multiple adsorption conformations can exist at the interface due to heterogeneous interactions raising from oil and water respectively. To further study the adsorption sites of the protein, the adsorption kinetics of OVA at the O/W interface is simulated using metadynamics method combined with CGMD simulations, and the result suggests the existence of multiple adsorption conformations of OVA at interface with the head-on conformation as the most stable one. In all, this work focuses on the adsorption behaviors of OVA at squalene/water interface, and provides a theoretical basis for further functionalization of the proteins in emulsion-based products and engineering.

Key words: Molecular dynamics simulation, Metadynamics, Protein adsorption, Structural stability, Ovalbumin

摘要： The adsorption of protein molecules to oil/water (O/W) interface is of critical importance for the product design in a wide range of technologies and industries such as biotechnology, food industry and pharmaceutical industry. In this work, with ovalbumin (OVA) as the model protein, the adsorption conformations at the O/W interface and the adsorption stability have been systematically studied via multiple simulation methods, including all-atom molecular dynamic (AAMD) simulations, coarse-grained molecular dynamic (CGMD) simulations and enhanced sampling methods. The computational results of AAMD and CGMD show that the hydrophobic tail of OVA tends to be folded under long time relaxation in aqueous phase, and multiple adsorption conformations can exist at the interface due to heterogeneous interactions raising from oil and water respectively. To further study the adsorption sites of the protein, the adsorption kinetics of OVA at the O/W interface is simulated using metadynamics method combined with CGMD simulations, and the result suggests the existence of multiple adsorption conformations of OVA at interface with the head-on conformation as the most stable one. In all, this work focuses on the adsorption behaviors of OVA at squalene/water interface, and provides a theoretical basis for further functionalization of the proteins in emulsion-based products and engineering.

关键词: Molecular dynamics simulation, Metadynamics, Protein adsorption, Structural stability, Ovalbumin

Qingxia Xiong, Ying Ren, Yufei Xia, Guanghui Ma, Reiji Noda, Wei Ge. Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface[J]. Chinese Journal of Chemical Engineering, 2022, 50(10): 369-378.

Qingxia Xiong, Ying Ren, Yufei Xia, Guanghui Ma, Reiji Noda, Wei Ge. Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface[J]. 中国化学工程学报, 2022, 50(10): 369-378.

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Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface

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