Structural understanding of stabilization patterns in engineered bispecific Ig‐like antibody molecules
Proteins Structure Function and Bioinformatics2009Vol. 77(4), pp. 832–841
Citations Over TimeTop 10% of 2009 papers
Jacob L. Jordan, Joseph W. Arndt, Karl J. M. Hanf, Guohui Li, Janine Hall, Stephen J. Demarest, Flora Huang, Xiufeng Wu, Brian Miller, Scott Glaser, Erik Fernández, Deping Wang, Alexey A. Lugovskoy
Abstract
Bispecific immunoglobulin-like antibodies capable of engaging multiple antigens represent a promising new class of therapeutic agents. Engineering of these molecules requires optimization of the molecular properties of one of the domain components. Here, we present a detailed crystallographic and computational characterization of the stabilization patterns in the lymphotoxin-beta receptor (LTbetaR) binding Fv domain of an anti-LTbetaR/anti-TNF-related apoptosis inducing ligand receptor-2 (TRAIL-R2) bispecific immunoglobulin-like antibody. We further describe a new hierarchical structure-guided approach toward engineering of antibody-like molecules to enhance their thermal and chemical stability.
Related Papers
- → Reduced elimination of IgG antibodies by engineering the variable region(2010)260 cited
- → Bispecific antibodies with natural architecture produced by co-culture of bacteria expressing two distinct half-antibodies(2013)197 cited
- → Production of Native Bispecific Antibodies in Rabbits(2010)20 cited
- → The use of Fab-Fc recombinant antibodies for studying the mechanism of triggering the effector activities of immunoglobulins(1984)1 cited
- → Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies(2023)1 cited