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Updated: Sep 2, 2025

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

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Antibody-Antigen Binding Interface Analysis in the Big Data Era

Pedro B P S Reis1,2, German P Barletta1,3,4, Luca Gagliardi1

  • 1CONCEPT Lab, Istituto Italiano di Teconologia, Genova, Italy.

Frontiers in Molecular Biosciences
|August 1, 2022
PubMed

Antibodies have become the Swiss Army tool for molecular biology and nanotechnology. Their outstanding ability to specifically recognise molecular antigens allows their use in many different applications from medicine to the industry. Moreover, the improvement of conventional structural biology techniques (e.g., X-ray, NMR) as well as the emergence of new ones (e.g., Cryo-EM), have permitted in the last years a notable increase of resolved antibody-antigen structures. This offers a unique opportunity to perform an exhaustive structural analysis of antibody-antigen interfaces by employing the large amount of data available nowadays. To leverage this factor, different geometric as well as chemical descriptors were evaluated to perform a comprehensive characterization.

Keywords:
antibody-antigen complexcomplementarity-determining region (CDR)epitope analysisparatope analysisstructure analysis and characterization

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