Quantifying antibody binding: techniques and therapeutic implications

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

Quantifying antibody binding: techniques and therapeutic implications

James Lodge, Lewis Kajtar, Rachel Duxbury, David Hall, Glenn A. Burley, Joanna Cordy, James W.T. Yates, Zahra Rattray^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

308 Downloads (Pure)

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.

Original language	English
Article number	2459795
Number of pages	20
Journal	mAbs
Volume	17
Issue number	1
Early online date	16 Feb 2025
DOIs	https://doi.org/10.1080/19420862.2025.2459795
Publication status	Published - 31 Dec 2025

Funding

The authors acknowledge GSK for funding a PhD studentship for J.L., R.D., L.K. via the University of Strathclyde Collaborative PhD programme. Z.R. and G.A.B. acknowledge funding from the UK Biotechnology and Biological Sciences Research Council (BB/Y003268/1).

Keywords

antibody
affinity
avidity
target engagement
pharmacology
pharmacokinetics

Access to Document

10.1080/19420862.2025.2459795Licence: CC BY 4.0

Lodge-etal-MABS-2025-Quantifying-antibody-binding-techniques-and-therapeuticFinal published version, 2.24 MBLicence: CC BY 4.0

A Prosperity Partnership for the Design of Next-Generation Antibody Drug Bioconjugates (Next-Gen ADC)
Burley, G. (Principal Investigator), Jamieson, C. (Co-investigator), Kerr, W. (Co-investigator), Nordon, A. (Co-investigator), Rattray, Z. (Co-investigator) & Tomkinson, N. (Co-investigator)
BBSRC (Biotech & Biological Sciences Research Council)
15/11/23 → 14/11/28
Project: Research

Cite this

@article{0388aadbd0b043919244a4b159499b4e,

title = "Quantifying antibody binding: techniques and therapeutic implications",

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.",

keywords = "antibody, affinity, avidity, target engagement, pharmacology, pharmacokinetics",

author = "James Lodge and Lewis Kajtar and Rachel Duxbury and David Hall and Burley, \{Glenn A.\} and Joanna Cordy and Yates, \{James W.T.\} and Zahra Rattray",

year = "2025",

month = dec,

day = "31",

doi = "10.1080/19420862.2025.2459795",

language = "English",

volume = "17",

number = "1",

}

TY - JOUR

T1 - Quantifying antibody binding

T2 - techniques and therapeutic implications

AU - Lodge, James

AU - Kajtar, Lewis

AU - Duxbury, Rachel

AU - Hall, David

AU - Burley, Glenn A.

AU - Cordy, Joanna

AU - Yates, James W.T.

AU - Rattray, Zahra

PY - 2025/12/31

Y1 - 2025/12/31

N2 - 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.

AB - 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.

KW - antibody

KW - affinity

KW - avidity

KW - target engagement

KW - pharmacology

KW - pharmacokinetics

U2 - 10.1080/19420862.2025.2459795

DO - 10.1080/19420862.2025.2459795

M3 - Article

VL - 17

JO - mAbs

JF - mAbs

IS - 1

M1 - 2459795

ER -

Quantifying antibody binding: techniques and therapeutic implications

Abstract

Funding

Keywords

Access to Document

Fingerprint

Projects

A Prosperity Partnership for the Design of Next-Generation Antibody Drug Bioconjugates (Next-Gen ADC)

Cite this