Analytical Method for Experimental Validation of Computer-Designed Antibody

In the computational design of antibodies, the interaction analysis between target antigen and antibody is an essential process to obtain feedback for validation and optimization of the design. Kinetic and thermodynamic parameters as well as binding affinity (K ) allow for a more detailed evaluation...

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Bibliographic Details
Published inMethods in molecular biology (Clifton, N.J.) Vol. 2552; p. 409
Main Authors Tanabe, Aki, Tsumoto, Kouhei
Format Journal Article
LanguageEnglish
Published United States 2023
Subjects
Antibodies
Antigens
Computers
Enzyme-Linked Immunosorbent Assay
Kinetics
Experimental validation
Kinetic parameters
Thermodynamic parameters
Affinity
Fluorescence polarization (FP)
Interaction analysis of antigen–antibody
Flow cytometry (FCM)
Biolayer interferometry (BLI)
ELISA
Microscale thermophoresis (MST)
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Summary:In the computational design of antibodies, the interaction analysis between target antigen and antibody is an essential process to obtain feedback for validation and optimization of the design. Kinetic and thermodynamic parameters as well as binding affinity (K ) allow for a more detailed evaluation and understanding of the molecular recognition. In this chapter, we summarize the conventional experimental methods which can calculate K value (ELISA, FP), analyze a binding activity to actual cells (FCM), and evaluate the kinetic and thermodynamic parameters (ITC, SPR, BLI), including high-throughput analysis and a recently developed experimental technique.
ISSN:1940-6029
DOI:10.1007/978-1-0716-2609-2_23