分子动力学模拟加热对肌动蛋白结构及酚类物质吸附的影响

帅雨桐 黄业传 何元琪 詹雅雯 孙梦

摘要：为研究不同加热温度对肌动蛋白结构及其对酚类物质吸附的影响，采用分子动力学模拟和分子对接技术研究25、80、100 ℃和120 ℃条件下，肌动蛋白结构的变化及其对6 种愈创木酚、1-辛烯-3-醇、1-辛烯-3-酮和2-辛烯醛吸附能力的影响。结果表明：随温度的升高，肌动蛋白构象变化均方根误差、均方根波动值明显增加，回旋半径波动增强且平衡后呈下降趋势，疏水区域溶剂可及表面积增大;随温度的升高，蛋白内部氢键数量减少，且120 ℃时最为显著。加热时蛋白α-螺旋和β-折叠含量显著下降而无规则卷曲结构含量显著升高。温度对1-辛烯-3-醇、1-辛烯-3-酮和2-辛烯醛的吸附没有显著影响，80 ℃和120 ℃时对酚类物质的吸附降低，100 ℃时与对照组相当，因此，相比其他加热条件，100 ℃加热更利于肌动蛋白对酚类物质的吸附;另外，肌动蛋白对酚类的吸附远大于同分子质量的醇、酮和醛类。

关键词：肌动蛋白;热处理;分子动力学;酚类物质;吸附

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）

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 （R_g） 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， theα-helix andβ-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.

Keywords： actin; heating; molecular dynamics; phenolic compounds; binding

DOI：10.7506/rlyj1001-8123-20210309-057

中圖分类号：TS251.1                   文献标志码：A               文章编号：

引文格式：

帅雨桐， 黄业传， 何元琪， 等. 分子动力学模拟加热对肌动蛋白结构及酚类物质吸附的影响[J]. 肉类研究， 2021， 35（3）：  . DOI：10.7506/rlyj1001-8123-20210309-057.    http：//www.rlyj.net.cn

SHUAI Yutong， HUANG Yechuan， HE Yuanqi， et al. Effect of heating on structure and phenolics binding capacity of actin studied using molecular dynamics simulation[J]. Meat Research， 2021， 35（3）：  . DOI：10.7506/rlyj1001-8123-20210309-057.    http：//www.rlyj.net.cn

风味是消费者评价肉制品品质的重要因素，川味腊肉由于其独特的烟熏风味深受消费者喜爱。这是由于川味腊肉加工过程中经过烟熏处理，不但使成品腊肉拥有独特风味，还具有杀菌、抗氧化、去腥、延长贮藏期等作用。烟熏特征风味主要由一些酚类物质构成，如烷基酚类、愈创木基型酚类、紫丁香基型酚类^[1]。……