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| Effect of Heating on Structure and Phenolics Binding Capacity of Actin Studied Using Molecular Dynamics Simulation |
| SHUAI Yutong, HUANG Yechuan, HE Yuanqi, ZHAN Yawen, SUN Meng |
| School of Life Science and Engineering, Southwest University of Science and Technology, Mianyang 621000, China |
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Abstract In order to study the effects of different heating temperatures on the structure and phenolic binding capacity of actin, molecular dynamics simulation and molecular docking were used to study the changes of actin structure at 25, 80, 100 and 120 ℃ and their effects on the binding capacity to six guaiacols, 1-octen-3-ol, 1-octen-3-one and 2-octenal. The results showed that the root mean square deviation (RMSD) and root mean square fluctuation (RMSF) of actin conformational changes increased significantly with the increase of temperature, the gyration radius (Rg) increased until reaching an equilibrium and then decreased, and the solvent accessible surface area of hydrophobic region increased. The number of hydrogen bonds in the protein gradually decreased with increasing temperature up to 120 ℃. After heat treatment, the α-helix and β-sheet contents in the protein decreased significantly, while the random coil content increased significantly. Temperature had no significant effect on the binding of 1-octen-3-ol, 1-octen-3-one and 2-octenal to actin; the binding capacity decreased at 80 and 120 ℃, but at 100 ℃ it was equivalent to that of the control group. Therefore, heating at 100 ℃ was more conducive to the binding of phenolics to protein than other heating conditions. In addition, the binding capacity of phenolics to actin was much greater than that of alcohols, ketones and aldehydes with the same molecular mass.
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2021, Vol. 35 
