Epitope Mapping of Antibodies
When an antibody binds to an antigen, it interacts with specific regions on the surface of the antigen known as epitopes. The binding of the antibody to the antigen can cause changes in the conformation and dynamics of the epitope, which can be detected by differences in the extent of deuterium exchange.
By comparing the deuterium exchange patterns in the epitope region of the antigen in the unbound and bound states, we can can identify the residues involved in the antibody-antigen interaction and map the antibody epitopes. This technique allows for rapid screening of multiple antibodies.
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We have worked with several researchers mapping antibody-antigen interfaces. A large portion of this research is currently unpublished.
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Epitope mapping of Antibodies
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Rathinaswamy MK*, Fleming KD*, Dalwadi U, Pardon E, Harris NJ, Yip CK, Steyaert J, Burke JE (2021) HDX-MS-optimized approach to characterize nanobodies as tools for biochemical and structural studies of class IB phosphoinositide 3-kinases. Structure
(CIHR)