光谱和计算综合分析揭示了农药谷硫磷与牛β-乳球蛋白的分子相互作用

IF 2.3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Nasser Abdulatif Al-Shabib, Javed Masood Khan, Ajamaluddin Malik, Abdulaziz AlAmri, Md Tabish Rehman, Mohamed F. AlAjmi, Fohad Mabood Husain
{"title":"光谱和计算综合分析揭示了农药谷硫磷与牛β-乳球蛋白的分子相互作用","authors":"Nasser Abdulatif Al-Shabib,&nbsp;Javed Masood Khan,&nbsp;Ajamaluddin Malik,&nbsp;Abdulaziz AlAmri,&nbsp;Md Tabish Rehman,&nbsp;Mohamed F. AlAjmi,&nbsp;Fohad Mabood Husain","doi":"10.1002/jmr.3086","DOIUrl":null,"url":null,"abstract":"<p>Organophosphorus are typically hazardous chemicals used in the pharmaceutical, agricultural, and other industries. They pose a serious risk to human life and can be fatal upon direct exposure. Hence, studying the interaction between such compounds with proteins is crucial for environmental, health, and food safety. In this study, we investigated the interaction mechanism between azinphos-methyl (AZM) and β-lactoglobulin (BLG) at pH 7.4 using a combination of biophysical techniques. Intrinsic fluorescence investigations revealed that BLG fluorescence was quenched in the presence of increasing AZM concentrations. The quenching mechanism was identified as static, as evidenced by a decrease in the fluorescence quenching constant (1.25 × 10<sup>4</sup>, 1.18 × 10<sup>4</sup>, and 0.86 × 10<sup>4</sup> M<sup>−1</sup>) with an increase in temperatures. Thermodynamic calculations (Δ<i>H</i> &gt; 0; Δ<i>S</i> &gt; 0) affirmed the formation of a complex between AZM and BLG through hydrophobic interactions. The BLG's secondary structure was found to be increased due to AZM interaction. Ultraviolet –visible spectroscopy data showed alterations in BLG conformation in the presence of AZM. Molecular docking highlighted the significant role of hydrophobic interactions involving residues such as Val43, Ile56, Ile71, Val92, Phe105, and Met107 in the binding between BLG and AZM. A docking energy of −6.9 kcal mol<sup>−1</sup>, and binding affinity of 1.15 × 10<sup>5</sup> M<sup>−1</sup> suggest spontaneous interaction between AZM and BLG with moderate to high affinity. These findings underscore the potential health risks associated with the entry of AZM into the food chain, emphasizing the need for further consideration of its impact on human health.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 4","pages":""},"PeriodicalIF":2.3000,"publicationDate":"2024-04-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Integrated spectroscopic and computational analyses unravel the molecular interaction of pesticide azinphos-methyl with bovine beta-lactoglobulin\",\"authors\":\"Nasser Abdulatif Al-Shabib,&nbsp;Javed Masood Khan,&nbsp;Ajamaluddin Malik,&nbsp;Abdulaziz AlAmri,&nbsp;Md Tabish Rehman,&nbsp;Mohamed F. AlAjmi,&nbsp;Fohad Mabood Husain\",\"doi\":\"10.1002/jmr.3086\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>Organophosphorus are typically hazardous chemicals used in the pharmaceutical, agricultural, and other industries. They pose a serious risk to human life and can be fatal upon direct exposure. Hence, studying the interaction between such compounds with proteins is crucial for environmental, health, and food safety. In this study, we investigated the interaction mechanism between azinphos-methyl (AZM) and β-lactoglobulin (BLG) at pH 7.4 using a combination of biophysical techniques. Intrinsic fluorescence investigations revealed that BLG fluorescence was quenched in the presence of increasing AZM concentrations. The quenching mechanism was identified as static, as evidenced by a decrease in the fluorescence quenching constant (1.25 × 10<sup>4</sup>, 1.18 × 10<sup>4</sup>, and 0.86 × 10<sup>4</sup> M<sup>−1</sup>) with an increase in temperatures. Thermodynamic calculations (Δ<i>H</i> &gt; 0; Δ<i>S</i> &gt; 0) affirmed the formation of a complex between AZM and BLG through hydrophobic interactions. The BLG's secondary structure was found to be increased due to AZM interaction. Ultraviolet –visible spectroscopy data showed alterations in BLG conformation in the presence of AZM. Molecular docking highlighted the significant role of hydrophobic interactions involving residues such as Val43, Ile56, Ile71, Val92, Phe105, and Met107 in the binding between BLG and AZM. A docking energy of −6.9 kcal mol<sup>−1</sup>, and binding affinity of 1.15 × 10<sup>5</sup> M<sup>−1</sup> suggest spontaneous interaction between AZM and BLG with moderate to high affinity. These findings underscore the potential health risks associated with the entry of AZM into the food chain, emphasizing the need for further consideration of its impact on human health.</p>\",\"PeriodicalId\":16531,\"journal\":{\"name\":\"Journal of Molecular Recognition\",\"volume\":\"37 4\",\"pages\":\"\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-04-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Recognition\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3086\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Recognition","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/jmr.3086","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

有机磷是典型的危险化学品,用于制药、农业和其他行业。它们对人类生命构成严重威胁,直接接触可致人死亡。因此,研究此类化合物与蛋白质之间的相互作用对环境、健康和食品安全至关重要。在这项研究中,我们采用多种生物物理技术研究了谷硫磷(AZM)与β-乳球蛋白(BLG)在 pH 7.4 下的相互作用机制。本征荧光研究表明,在 AZM 浓度增加的情况下,BLG 的荧光会被淬灭。荧光淬灭常数(1.25 × 104、1.18 × 104 和 0.86 × 104 M-1)随着温度的升高而降低,这证明淬灭机制是静态的。热力学计算(ΔH > 0; ΔS > 0)证实了 AZM 和 BLG 通过疏水作用形成了复合物。研究发现,由于 AZM 的相互作用,BLG 的二级结构有所增加。紫外-可见光谱数据显示,在 AZM 的存在下,BLG 的构象发生了改变。分子对接突显了涉及 Val43、Ile56、Ile71、Val92、Phe105 和 Met107 等残基的疏水相互作用在 BLG 与 AZM 之间的结合中的重要作用。对接能为 -6.9 kcal mol-1,结合亲和力为 1.15 × 105 M-1,这表明 AZM 和 BLG 之间存在自发的相互作用,亲和力为中度至高度。这些发现凸显了 AZM 进入食物链可能带来的健康风险,强调有必要进一步考虑其对人类健康的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Integrated spectroscopic and computational analyses unravel the molecular interaction of pesticide azinphos-methyl with bovine beta-lactoglobulin

Organophosphorus are typically hazardous chemicals used in the pharmaceutical, agricultural, and other industries. They pose a serious risk to human life and can be fatal upon direct exposure. Hence, studying the interaction between such compounds with proteins is crucial for environmental, health, and food safety. In this study, we investigated the interaction mechanism between azinphos-methyl (AZM) and β-lactoglobulin (BLG) at pH 7.4 using a combination of biophysical techniques. Intrinsic fluorescence investigations revealed that BLG fluorescence was quenched in the presence of increasing AZM concentrations. The quenching mechanism was identified as static, as evidenced by a decrease in the fluorescence quenching constant (1.25 × 104, 1.18 × 104, and 0.86 × 104 M−1) with an increase in temperatures. Thermodynamic calculations (ΔH > 0; ΔS > 0) affirmed the formation of a complex between AZM and BLG through hydrophobic interactions. The BLG's secondary structure was found to be increased due to AZM interaction. Ultraviolet –visible spectroscopy data showed alterations in BLG conformation in the presence of AZM. Molecular docking highlighted the significant role of hydrophobic interactions involving residues such as Val43, Ile56, Ile71, Val92, Phe105, and Met107 in the binding between BLG and AZM. A docking energy of −6.9 kcal mol−1, and binding affinity of 1.15 × 105 M−1 suggest spontaneous interaction between AZM and BLG with moderate to high affinity. These findings underscore the potential health risks associated with the entry of AZM into the food chain, emphasizing the need for further consideration of its impact on human health.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Journal of Molecular Recognition
Journal of Molecular Recognition 生物-生化与分子生物学
CiteScore
4.60
自引率
3.70%
发文量
68
审稿时长
2.7 months
期刊介绍: Journal of Molecular Recognition (JMR) publishes original research papers and reviews describing substantial advances in our understanding of molecular recognition phenomena in life sciences, covering all aspects from biochemistry, molecular biology, medicine, and biophysics. The research may employ experimental, theoretical and/or computational approaches. The focus of the journal is on recognition phenomena involving biomolecules and their biological / biochemical partners rather than on the recognition of metal ions or inorganic compounds. Molecular recognition involves non-covalent specific interactions between two or more biological molecules, molecular aggregates, cellular modules or organelles, as exemplified by receptor-ligand, antigen-antibody, nucleic acid-protein, sugar-lectin, to mention just a few of the possible interactions. The journal invites manuscripts that aim to achieve a complete description of molecular recognition mechanisms between well-characterized biomolecules in terms of structure, dynamics and biological activity. Such studies may help the future development of new drugs and vaccines, although the experimental testing of new drugs and vaccines falls outside the scope of the journal. Manuscripts that describe the application of standard approaches and techniques to design or model new molecular entities or to describe interactions between biomolecules, but do not provide new insights into molecular recognition processes will not be considered. Similarly, manuscripts involving biomolecules uncharacterized at the sequence level (e.g. calf thymus DNA) will not be considered.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信