{"title":"不同电荷肽对α-淀粉酶的影响及其相互作用机制分析","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":"<p><p>Nowadays α-amylase is widely used in various fields. Therefore, in this study, the effects of neutral (T<sub>0</sub>), negatively charged (T<sub>8</sub><sup>-</sup>) and positively charged (T<sub>9</sub><sup>+</sup>) 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 T<sub>8</sub><sup>-</sup> and T<sub>9</sub><sup>+</sup> increasing and decreasing α-amylase activity, respectively, whereas T<sub>0</sub> 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.</p>","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":"{\"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\":\"<p><p>Nowadays α-amylase is widely used in various fields. Therefore, in this study, the effects of neutral (T<sub>0</sub>), negatively charged (T<sub>8</sub><sup>-</sup>) and positively charged (T<sub>9</sub><sup>+</sup>) 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 T<sub>8</sub><sup>-</sup> and T<sub>9</sub><sup>+</sup> increasing and decreasing α-amylase activity, respectively, whereas T<sub>0</sub> 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.</p>\",\"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}","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}
Analysis of the effects of differently charged peptides on α-amylase and their interaction mechanisms.
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.
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.
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