Quantifying antibody binding: techniques and therapeutic implications.

IF 7.3 2区 医学 Q1 MEDICINE, RESEARCH & EXPERIMENTAL mAbs Pub Date : 2025-12-01 Epub Date: 2025-02-16 DOI:10.1080/19420862.2025.2459795
James Lodge, Lewis Kajtar, Rachel Duxbury, David Hall, Glenn A Burley, Joanna Cordy, James W T Yates, Zahra Rattray
{"title":"Quantifying antibody binding: techniques and therapeutic implications.","authors":"James Lodge, Lewis Kajtar, Rachel Duxbury, David Hall, Glenn A Burley, Joanna Cordy, James W T Yates, Zahra Rattray","doi":"10.1080/19420862.2025.2459795","DOIUrl":null,"url":null,"abstract":"<p><p>The binding kinetics of an antibody for its target antigen represent key determinants of its biological function and success as a novel biotherapeutic. Defining these interactions and kinetics is critical for understanding the pharmacological and pharmacodynamic profiles of antibodies in therapeutic applications, with line of sight to clinical translation. In this review, we discuss the latest developments in approaches to measure and modulate antibody-antigen interactions, including antibody engineering, novel antibody formats, current, and emerging technologies for measuring antibody-antigen binding interactions, and emerging perspectives within the field. We also explore how emerging computational methods are set to become powerful tools for modeling antibody-binding interactions under physiologically relevant conditions. Finally, we consider the therapeutic implications of modulating target engagement in terms of pharmacodynamics and pharmacokinetics.</p>","PeriodicalId":18206,"journal":{"name":"mAbs","volume":"17 1","pages":"2459795"},"PeriodicalIF":7.3000,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11834528/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"mAbs","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.1080/19420862.2025.2459795","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/2/16 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"MEDICINE, RESEARCH & EXPERIMENTAL","Score":null,"Total":0}
引用次数: 0

Abstract

The binding kinetics of an antibody for its target antigen represent key determinants of its biological function and success as a novel biotherapeutic. Defining these interactions and kinetics is critical for understanding the pharmacological and pharmacodynamic profiles of antibodies in therapeutic applications, with line of sight to clinical translation. In this review, we discuss the latest developments in approaches to measure and modulate antibody-antigen interactions, including antibody engineering, novel antibody formats, current, and emerging technologies for measuring antibody-antigen binding interactions, and emerging perspectives within the field. We also explore how emerging computational methods are set to become powerful tools for modeling antibody-binding interactions under physiologically relevant conditions. Finally, we consider the therapeutic implications of modulating target engagement in terms of pharmacodynamics and pharmacokinetics.

Abstract Image

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
定量抗体结合:技术和治疗意义。
抗体与其靶抗原的结合动力学是决定其生物学功能和作为一种新型生物治疗药物成功与否的关键因素。定义这些相互作用和动力学对于理解抗体在治疗应用中的药理学和药效学特征至关重要,并有助于临床转化。在这篇综述中,我们讨论了测量和调节抗体-抗原相互作用方法的最新进展,包括抗体工程,新型抗体格式,当前和新兴的测量抗体-抗原结合相互作用的技术,以及该领域的新兴观点。我们还探讨了如何将新兴的计算方法设置为在生理相关条件下模拟抗体结合相互作用的强大工具。最后,我们考虑在药效学和药代动力学方面调节靶标接合的治疗意义。
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 去求助
来源期刊
mAbs
mAbs 工程技术-仪器仪表
CiteScore
10.70
自引率
11.30%
发文量
77
审稿时长
6-12 weeks
期刊介绍: mAbs is a multi-disciplinary journal dedicated to the art and science of antibody research and development. The journal has a strong scientific and medical focus, but also strives to serve a broader readership. The articles are thus of interest to scientists, clinical researchers, and physicians, as well as the wider mAb community, including our readers involved in technology transfer, legal issues, investment, strategic planning and the regulation of therapeutics.
期刊最新文献
Rapid and selective characterization of antibody-drug conjugates in complex sample matrices by native affinity liquid chromatography-mass spectrometry. Alpseq: an open-source workflow to turbocharge nanobody discovery with high-throughput sequencing. Balancing the extremes for antibody developability: hydrophobic and electrostatic germline framework signatures for CDR-loop compensation. NAStructuralDB : structural database to facilitate computational studies of molecular modeling and recognition of proteins with special focus on antibody-antigen interactions. Impact of process parameters on IgG glycosylation in CHO systems: a comprehensive quantitative analysis.
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1