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Characterization of Monoclonal Antibody - Protein Antigen Complexes Using Small-Angle Scattering and Molecular Modeling
Published
Author(s)
Maria Monica Castellanos Mantilla, James Anthony Snyder, Melody Lee, Srinivas Chakravarthy, Nicholas J. Clark, Arnold McAuley, Joseph E. Curtis
Abstract
The determination of monoclonal antibody interactions with protein antigens in solution can lead to important insight to guide physical characterization and molecular engineering of therapeutic targets. We used small-angle scattering (SAS) combined with size-exclusion multi-angle light scattering high-performance liquid chromatography to obtain monodisperse samples with defined stoichometry to study an antio-streptavidin monodentate and bidentate antibody - antigen complexes were generated using molecular docking protocols and molecular docking protocols and molecular simulations. By comparing theoretical SAS profiles to the experimental data it was determined that the primary component(s) were compact monodentate and/or bidentate complexes. SAS profiles of extended monodentate complexes were not consistent with the experimental data. These results highlight the capability to determine the shape of monoclonal antibody - antigen complexes in solution using SAS data and physics-based molecular modeling.
Castellanos Mantilla, M.
, Snyder, J.
, Lee, M.
, Chakravarthy, S.
, Clark, N.
, McAuley, A.
and Curtis, J.
(2017),
Characterization of Monoclonal Antibody - Protein Antigen Complexes Using Small-Angle Scattering and Molecular Modeling, Antibodies, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=924842
(Accessed October 8, 2025)