Article in Journal of Computer-Aided Molecular Design vol. 37, 201-215

Nancy D. Pomarici, Franz Waibl, Patrick K. Quoika, Alexander Bujotzek, Guy Georges, Monica L. Fernández-Quintero and Klaus R. Liedl, Structural mechanism of Fab domain dissociation as a measure of interface stability

By Nancy Pomarici

We are pleased to present a new article by N. Pomarici, F. Waibl, P. Quoika, A. Bujotzek, G. Georges, M. Fernández-Quintero and K. Liedl about stability of the antigen binding fragments in monoclonal antibodies. In this work, the authors study how different pairings of heavy and light chain germlines influence the stability of Fab fragments, using molecular dynamics simulations. They reveal that the CDR loops, together with the interface interactions, play a central role in stabilizing the overall structure. This study can have a massive impact on the design of novel and better performing biotherapeutics.

 
For more information: https://doi.org/10.1007/s10822-023-00501-9


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