Epitope Mapping

Epitope Mapping designates techniques identifying specific molecular regions recognised by antibodies or T-cell receptors, providing detailed characterisation of antigen-antibody interactions essential for therapeutic antibody development, vaccine design, diagnostic assay optimisation, and understanding immune responses. Epitopes comprise continuous sequences of amino acids or discontinuous residues brought together through protein folding.

The biopharmaceutical industry employs epitope mapping throughout therapeutic antibody and vaccine development. Antibody characterisation requires epitope mapping confirming binding sites, assessing uniqueness, predicting potential resistance mutations, and supporting intellectual property claims. Biosimilar development uses epitope mapping demonstrating similar binding to reference products. Epitope binning groups antibodies recognising distinct epitopes, enabling selection of non-competing pairs for bispecific antibody development. Methods include peptide scanning, hydrogen-deuterium exchange mass spectrometry, alanine scanning mutagenesis, and structure determination. As antibody therapeutics proliferate and vaccines advance towards structure-based design, epitope mapping remains critical technology informing rational development.