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探索牛磺酸对尿酸氧化酶生化特性的影响：响应面法和分子动力学模拟

Exploring the impact of taurine on the biochemical properties of urate oxidase: response surface methodology and molecular dynamics simulation.

作者信息

Shahmoradipour Parisa, Zaboli Maryam, Torkzadeh-Mahani Masoud

机构信息

Department of Biotechnology, , Institute of Science, High Technology and Environmental Sciences, Graduate University of Advanced Technology, Kerman, Iran.

Department of chemistry, faculty of science, University of Birjand, Birjand, Iran.

出版信息

J Biol Eng. 2024 Jan 22;18(1):10. doi: 10.1186/s13036-023-00397-x.

DOI:10.1186/s13036-023-00397-x
PMID:38254151
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10804793/
Abstract

This paper investigates the impact of taurine as an additive on the structural and functional stability of urate oxidase. First, the effect of the processing parameters for the stabilization of Urate Oxidase (UOX) using taurine was examined using the response surface methodology (RSM) and the central composite design (CCD) model. Also, the study examines thermodynamic and kinetic parameters as well as structural changes of urate oxidase with and without taurine. Fluorescence intensity changes indicated static quenching during taurine binding. The obtained result indicates that taurine has the ability to preserve the native structural conformation of UOX. Furthermore, molecular dynamics simulation is conducted in order to get insights into the alterations in the structure of urate oxidase in the absence and presence of taurine under optimal conditions. The molecular dynamics simulation section investigated the formation of hydrogen bonds (H-bonds) between different components as well as analysis of root mean square deviation (RMSD), root mean square fluctuations (RMSF) and secondary structure. Lower Cα-RMSD and RMSF values indicate greater stabilization of the taurine-treated UOX structure compared to the free enzyme. The results of molecular docking indicate that the binding of taurine to the UOX enzyme through hydrophobic interactions is associated with a negative value for the Gibbs free energy.

摘要

本文研究了牛磺酸作为添加剂对尿酸氧化酶结构和功能稳定性的影响。首先，使用响应面法（RSM）和中心复合设计（CCD）模型研究了牛磺酸稳定尿酸氧化酶（UOX）的工艺参数的影响。此外，该研究还考察了有无牛磺酸时尿酸氧化酶的热力学和动力学参数以及结构变化。荧光强度变化表明牛磺酸结合过程中发生了静态猝灭。所得结果表明，牛磺酸具有保留UOX天然结构构象的能力。此外，进行分子动力学模拟以深入了解在最佳条件下有无牛磺酸时尿酸氧化酶结构的变化。分子动力学模拟部分研究了不同组分之间氢键（H键）的形成以及均方根偏差（RMSD）、均方根波动（RMSF）和二级结构分析。较低的Cα-RMSD和RMSF值表明与游离酶相比，牛磺酸处理的UOX结构具有更高的稳定性。分子对接结果表明，牛磺酸通过疏水相互作用与UOX酶结合，其吉布斯自由能为负值。

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