Computational Model-assisted Carbohydrate Antibody Domain Glycosylation Service

Computational Model-assisted Carbohydrate Antibody Domain Glycosylation Service

Computational Design of Specific Functional Antibodies

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.

Antibody constant (Fc) domain glycosylation

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.

Antibody variable (Fv) domain glycosylation

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.

Flowchart of carbohydrate antibody domain glycosylation. (CD BioGlyco)

Publication

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 Conserved interface residues with importance for VH/VL association. Fig.1 Schematic illustration of conserved interfacial amino acids. (Herold, et al., 2017)

Applications

  • Computational model-assisted carbohydrate antibody domain glycosylation can be used to modulate activity in drug development.
  • Computational model-assisted carbohydrate antibody domain glycosylation can be used to produce antibodies for specific therapeutic effects.
  • Computational model-assisted carbohydrate antibody domain glycosylation can be used to develop targeted cytokine therapies.

Advantages of Us

  • Our researchers are very skilled in Fc modification and we provide modified antibodies with strong effector functions and extended half-life.
  • We have an experienced computational modeling team to solve all the problems of carbohydrate antibody modification for our clients.

Frequently Asked Questions

  • Does the modified antibody affect its original activity?
    • The modified antibody does not affect its original activity. The purpose of modification and transformation is to introduce a new activity or to amplify the original activity. If the client needs to silence the original activity, we also provide the corresponding modification service.
  • What role does antibody glycosylation play in immunization?
    • Glycosylation of antibodies plays an important role in immunotherapy such as enhancing the antibody-dependent cellular cytotoxicity (ADCC) and complement-activated complement-dependent cytotoxicity (CDC) function of antibodies, shielding molecules from immunogenicity, increasing half-life in vivo, and so on.

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.

Reference

  1. Herold, E.M.; et al. Determinants of the assembly and function of antibody variable domains. Scientific Reports. 2017, 7(1): 12276.
For research use only. Not intended for any diagnostic use.
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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.

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