基于虚拟筛选、分子对接和分子互作解析两种大球盖菇十肽的呈味特性和ACE抑制活性作用机制  

Exploring the Taste Characteristics and ACE-inhibitory Active Mechanism of Stropharia rugosoannulata Decapeptides Based on Virtual Screening,Molecular Docking,and Molecular Interactions

作　　者：李文[1,2] 陈万超[1] 马海乐[2] 吴迪[1] 张忠[1] 杨焱[1] LI Wen;CHEN Wanchao;MA Haile;WU Di;ZHANG Zhong;YANG Yan(Institute of Edible Fungi,Shanghai Academy of Agricultural Sciences,Shanghai 201403,China;School of Food&Biological Engineering,Jiangsu University,Zhenjiang 212013,China)

机构地区：[1]上海市农业科学院食用菌研究所,上海201403 [2]江苏大学食品与生物工程学院,江苏镇江212013

出　　处：《食品工业科技》2023年第20期11-17,共7页Science and Technology of Food Industry

基　　金：上海市科技兴农项目(2020-02-08-00-12-F01484)。

摘　　要：为探究大球盖菇十肽的呈味特性和潜在的生物活性,以两种大球盖菇十肽(RIEDNLVIIR和SLPIKPRVPF)为研究对象,采用虚拟筛选、分子对接和分子互作技术,对两种大球盖菇十肽的呈味特性和ACE抑制活性作用机制进行预测和验证。结果显示,两种大球盖菇十肽均具有咸鲜呈味肽片段和ACE抑制活性肽片段。RIEDN-LVIIR具有咸味呈味特性,SLPIKPRVPF具有鲜味呈味特性。两种大球盖菇十肽可与ACE靶标蛋白受体结合形成氢键和静电相互作用。体外活性验证结果表明,大球盖菇咸味十肽RIEDNLVIIR的ACE抑制效果较好,IC_(50)值为0.012 mg/mL。分子互作热力学和动力学结果显示,RIEDNLVIIR与ACE受体之间结合是焓驱动反应的特异性结合。虚拟筛选活性预测结果、体外活性验证结果、及分子对接和分子互作的ACE抑制机制解析结果具有一致性。研究为理解大球盖菇十肽呈味特性和ACE抑制活性作用机制提供理论依据,为具有ACE抑制活性的大球盖菇咸鲜味十肽在健康调味品和功能产品中的应用奠定基础。To explore the taste characteristics and potential biological activities of the decapeptides of Stropharia rugosoannulata,two decapeptides(RIEDNLVIIR and SLPIKPRVPF)were selected to predict and validate the taste-presenting properties and ACE inhibitory activity mechanism by using virtual screening,molecular docking,and molecular interactions techniques.The results showed that the two decapeptides of S.rugosoannulata all had salty and umami tastes and ACE-inhibited peptide fragments.RIEDNLVIR had a salty taste,and SLPIKPRVPF had an umami taste.Two decapeptides of S.rugosoannulata could strongly bind to ACE receptors to form hydrogen bonds and electrostatic interactions.The in vitro activity validation results showed that the salty decapeptide RIEDNLVIIR inhibited the ACE well with an IC_(50) value of 0.012 mg/mL.The molecular interaction thermodynamics and kinetics results showed that the binding between RIEDNLVIR and ACE receptor was the specific binding of enthalpy-driven reaction.The results of virtual screening activity prediction,in vitro activity validation,and molecular docking and molecular interactions for ACE inhibition mechanism analysis were consistent.The study provides a theoretical basis for understanding the taste characteristics and ACE inhibition mechanism of S.rugosoannulata decapeptides and lays a foundation for applying the decapeptides with ACE inhibitory activity in healthy condiments and functional products.

关 键 词：大球盖菇十肽 分子对接 分子热力学 分子动力学 ACE抑制机制 

分 类 号：TS201.4[轻工技术与工程—食品科学]