Article in Protein Engineering, Design and Selection, Volume 35, 2022,

Nancy D. Pomarici, Monica L. Fernández-Quintero, Patrick K. Quoika, Franz Waibl, Alexander Bujotzek, Guy Georges and Klaus R. Liedl, Bispecific antibodies — effects of point mutations on CH3-CH3 interface stability

By Nancy Pomarici

How can we improve the development of novel biotherapeutics, as antibodies?

N. Pomarici et al. apply computational methods to investigate the stability of bispecific antibodies. The focus is on the last domains of the immunoglobulins, the CH3-CH3 domains, which have been previously engineered to achieve chain heterodimerization. In this work, the authors describe the mechanism of dissociation of the dimer and reveal key residues that stabilize the interface and thus advance the stability of the structure.


For more information: https://doi.org/10.1093/protein/gzac012

 



Nach oben scrollen