Combining glycan engineering and Computational Modeling, CD BioGlyco provides our clients with specialized Carbohydrate Antibody Development services. The different glycosylation patterns of the variable structural domains reflect specific immunomodulatory effects. Our active computational team provides clients with antibody glycosylation pattern modification services for modulating the biological activity of antibodies. In short, our researchers use highly accurate computational tools to introduce atypical glycosylation into antibodies to achieve the desired effect.
Upon antigen-antibody binding, the conformation of the Fc segment of the antibody is altered and produces a variety of biological effects. The Fc structural domain carries one or more conserved N-glycans. The binding of the Fc structural domain to the receptor is affected by glycosylation at the N297 position. Our researchers provide antibodies with specific functions by glycosylation of Fc fragments.
Relying on specific glycosylation modeling, we offer silencing, knockout, and introduction of the following modifications including but not limited to mannosylation, sialylation, galactosylation, and fucosylation.
CD BioGlyco provides complete antibody Fv glycosylation modification services including variant prediction, design, and activity evaluation. Integrating sequence, computational, and structural prediction information, our team installs a variety of N-glycosylation consensus sequences into antibody variable domains to provide clients with glyco-variants of atypical glycans.
Technology: Molecular dynamics simulations, Fluorescence spectroscopy
Journal: Scientific Reports
Published: 2017
IF: 3.8
Results: In this study, researchers performed a comprehensive analysis of the variable structure domains VL and VH of the antibody Fv module. Combining advanced computational tools and modeling, the researchers exchanged framework residues and CDR loops and analyzed the effect of the two Fvs with moderate affinity. Moreover, the study found that changes in CDR altered the variable domain framework. Analysis of two different pairs of variable domains in human and mouse antibodies revealed a relationship between antibody stability and the stability of the interface between the variable domains.
Fig.1 Schematic illustration of conserved interfacial amino acids. (Herold, et al., 2017)
CD BioGlyco provides highly active carbohydrate antibody modification services to help our clients further elucidate conformational relationships. Our staff is highly energetic and enthusiastic to fulfill each task with great care. For any further information, do not hesitate to contact us.
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We envision a future where the intricate world of carbohydrate is no longer shrouded in mystery, but rather illuminated by the power of cutting-edge computational tools.