Analysis of the effects of differently charged peptides on α-amylase and their interaction mechanisms.

IF 4.5 2区医学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Bioorganic Chemistry Pub Date : 2024-11-16 DOI:10.1016/j.bioorg.2024.107972

Xiaoyu Yang, Chuanbo Li, Qi Yang, Jiayi Ji, Xinyue Jiang, Chunying Liu, Fubao Sun, Xiaodan Wang, Shaohua Dou

{"title":"Analysis of the effects of differently charged peptides on α-amylase and their interaction mechanisms.","authors":"Xiaoyu Yang, Chuanbo Li, Qi Yang, Jiayi Ji, Xinyue Jiang, Chunying Liu, Fubao Sun, Xiaodan Wang, Shaohua Dou","doi":"10.1016/j.bioorg.2024.107972","DOIUrl":null,"url":null,"abstract":"Nowadays α-amylase is widely used in various fields. Therefore, in this study, the effects of neutral (T0), negatively charged (T8-) and positively charged (T9+) peptides on α-amylase activity were investigated by means of an applied protein electric field, and spectroscopy and molecular dynamics were employed to investigate this mechanism. It was found that the nature of the charge of the peptides had a strong influence on α-amylase activity, with T8- and T9+ increasing and decreasing α-amylase activity, respectively, whereas T0 had no effect on enzyme activity. Fluorescence spectroscopy and circular dichroism results indicated that the charged peptides changed the conformation of α-amylase. Meanwhile, the molecular dynamics results showed that the charged peptides changed the distribution of the surface charge of α-amylase mainly through electrostatic force, which not only changed the conformation of the enzyme, but also altered the microenvironment of the enzyme active centre, which caused α-amylase to become compact or loose to affect the enzyme activity.","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"153 ","pages":"107972"},"PeriodicalIF":4.5000,"publicationDate":"2024-11-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioorganic Chemistry","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1016/j.bioorg.2024.107972","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}

引用次数: 0

Abstract

Nowadays α-amylase is widely used in various fields. Therefore, in this study, the effects of neutral (T₀), negatively charged (T₈^-) and positively charged (T₉⁺) peptides on α-amylase activity were investigated by means of an applied protein electric field, and spectroscopy and molecular dynamics were employed to investigate this mechanism. It was found that the nature of the charge of the peptides had a strong influence on α-amylase activity, with T₈^- and T₉⁺ increasing and decreasing α-amylase activity, respectively, whereas T₀ had no effect on enzyme activity. Fluorescence spectroscopy and circular dichroism results indicated that the charged peptides changed the conformation of α-amylase. Meanwhile, the molecular dynamics results showed that the charged peptides changed the distribution of the surface charge of α-amylase mainly through electrostatic force, which not only changed the conformation of the enzyme, but also altered the microenvironment of the enzyme active centre, which caused α-amylase to become compact or loose to affect the enzyme activity.

查看原文本刊更多论文

不同电荷肽对α-淀粉酶的影响及其相互作用机制分析

如今，α-淀粉酶被广泛应用于各个领域。因此，本研究通过外加蛋白质电场研究了中性（T0）、带负电荷（T8-）和带正电荷（T9+）的多肽对α-淀粉酶活性的影响，并利用光谱学和分子动力学研究了这一机制。研究发现，肽的电荷性质对α-淀粉酶活性有很大影响，T8-和T9+分别会提高和降低α-淀粉酶活性，而T0对酶活性没有影响。荧光光谱和圆二色性结果表明，带电肽改变了α-淀粉酶的构象。同时，分子动力学结果表明，带电肽主要通过静电力改变了α-淀粉酶表面电荷的分布，不仅改变了酶的构象，还改变了酶活性中心的微环境，使α-淀粉酶变得紧密或疏松，从而影响了酶的活性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Bioorganic Chemistry 生物-生化与分子生物学

CiteScore

9.70

自引率

3.90%

发文量

679

审稿时长

31 days

期刊介绍： Bioorganic Chemistry publishes research that addresses biological questions at the molecular level, using organic chemistry and principles of physical organic chemistry. The scope of the journal covers a range of topics at the organic chemistry-biology interface, including: enzyme catalysis, biotransformation and enzyme inhibition; nucleic acids chemistry; medicinal chemistry; natural product chemistry, natural product synthesis and natural product biosynthesis; antimicrobial agents; lipid and peptide chemistry; biophysical chemistry; biological probes; bio-orthogonal chemistry and biomimetic chemistry. For manuscripts dealing with synthetic bioactive compounds, the Journal requires that the molecular target of the compounds described must be known, and must be demonstrated experimentally in the manuscript. For studies involving natural products, if the molecular target is unknown, some data beyond simple cell-based toxicity studies to provide insight into the mechanism of action is required. Studies supported by molecular docking are welcome, but must be supported by experimental data. The Journal does not consider manuscripts that are purely theoretical or computational in nature. The Journal publishes regular articles, short communications and reviews. Reviews are normally invited by Editors or Editorial Board members. Authors of unsolicited reviews should first contact an Editor or Editorial Board member to determine whether the proposed article is within the scope of the Journal.