Molecular dynamics simulations of ovalbumin adsorption at squalene/water interface  

作　　者：Qingxia Xiong Ying Ren Yufei Xia Guanghui Ma Reiji Noda Wei Ge 

机构地区：[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

出　　处：《Chinese Journal of Chemical Engineering》2022年第10期369-378,共10页中国化学工程学报（英文版）

基　　金：financially supported by the National Natural Science Foundation of China(Nos.21821005,21973097,92034302,91834303);the Innovation Academy for Green Manufacture,Chinese Academy of Sciences(IAGM-2019-A03,IAGM-2019-A13);Key Research Program of Frontier Science,Chinese Academy of Sciences(QYZDJ-SSW-JSC029)。

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 dynamicssimulation METADYNAMICS Protein adsorption Structural stability OVALBUMIN 

分 类 号：TQ931[化学工程]