利用计算机辅助蛋白-蛋白对接技术研究氨苄西林抗体与检测干扰蛋白的相互作用

Minghua Wang, Jianping Wang
{"title":"利用计算机辅助蛋白-蛋白对接技术研究氨苄西林抗体与检测干扰蛋白的相互作用","authors":"Minghua Wang, Jianping Wang","doi":"10.1109/BICTA.2010.5645093","DOIUrl":null,"url":null,"abstract":"It is important to study non-specific interaction between immobilized biomolecule and interferential proteins for biosensor development and commercialization. The advances in Bioinformatics and computer technology light up the in-depth understand of biological interaction. We use two different protein-protein docking program to simulate the non-specific interaction between ampicillin antibody and HSA (Human Serum Albumin). To evaluate the association probability of antibody active site, different amino acid chains and a well-known specific immune-complex were used to simulation. The result showed that the cluster density of non-specific interaction is smaller than specific interaction between lysozyme and antibody, and dock scores are scattered. The antibody active site is favourable to be influenced by non-specific protein interaction. The interaction strength of special manner was different in specific and non-specific bindings. It provides a probability for detection conditions adjusting improved in control non-specific adsorption of biosensor analytical process.","PeriodicalId":302619,"journal":{"name":"2010 IEEE Fifth International Conference on Bio-Inspired Computing: Theories and Applications (BIC-TA)","volume":"8 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2010-11-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Study on interaction between ampicillin antibody and detection interfering proteins by computer aided protein-protein docking for biosensor interesting\",\"authors\":\"Minghua Wang, Jianping Wang\",\"doi\":\"10.1109/BICTA.2010.5645093\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"It is important to study non-specific interaction between immobilized biomolecule and interferential proteins for biosensor development and commercialization. The advances in Bioinformatics and computer technology light up the in-depth understand of biological interaction. We use two different protein-protein docking program to simulate the non-specific interaction between ampicillin antibody and HSA (Human Serum Albumin). To evaluate the association probability of antibody active site, different amino acid chains and a well-known specific immune-complex were used to simulation. The result showed that the cluster density of non-specific interaction is smaller than specific interaction between lysozyme and antibody, and dock scores are scattered. The antibody active site is favourable to be influenced by non-specific protein interaction. The interaction strength of special manner was different in specific and non-specific bindings. It provides a probability for detection conditions adjusting improved in control non-specific adsorption of biosensor analytical process.\",\"PeriodicalId\":302619,\"journal\":{\"name\":\"2010 IEEE Fifth International Conference on Bio-Inspired Computing: Theories and Applications (BIC-TA)\",\"volume\":\"8 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2010-11-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"2010 IEEE Fifth International Conference on Bio-Inspired Computing: Theories and Applications (BIC-TA)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1109/BICTA.2010.5645093\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"2010 IEEE Fifth International Conference on Bio-Inspired Computing: Theories and Applications (BIC-TA)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/BICTA.2010.5645093","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

研究固定化生物分子与干扰蛋白之间的非特异性相互作用对生物传感器的开发和商业化具有重要意义。生物信息学和计算机技术的进步照亮了对生物相互作用的深入理解。我们使用两种不同的蛋白-蛋白对接程序模拟氨苄西林抗体与人血清白蛋白(HSA)的非特异性相互作用。为了评估抗体活性位点的关联概率,采用不同的氨基酸链和已知的特异性免疫复合物进行模拟。结果表明,溶菌酶与抗体非特异性相互作用的聚类密度小于特异性相互作用的聚类密度,且聚类得分较为分散。抗体活性位点容易受到非特异性蛋白相互作用的影响。特殊方式的交互强度在特定绑定和非特定绑定中是不同的。为控制生物传感器分析过程的非特异性吸附,改善检测条件提供了可能性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Study on interaction between ampicillin antibody and detection interfering proteins by computer aided protein-protein docking for biosensor interesting
It is important to study non-specific interaction between immobilized biomolecule and interferential proteins for biosensor development and commercialization. The advances in Bioinformatics and computer technology light up the in-depth understand of biological interaction. We use two different protein-protein docking program to simulate the non-specific interaction between ampicillin antibody and HSA (Human Serum Albumin). To evaluate the association probability of antibody active site, different amino acid chains and a well-known specific immune-complex were used to simulation. The result showed that the cluster density of non-specific interaction is smaller than specific interaction between lysozyme and antibody, and dock scores are scattered. The antibody active site is favourable to be influenced by non-specific protein interaction. The interaction strength of special manner was different in specific and non-specific bindings. It provides a probability for detection conditions adjusting improved in control non-specific adsorption of biosensor analytical process.
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
自引率
0.00%
发文量
0
×
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:604180095
Book学术官方微信