Blocking N-Glycan-Protein Interaction Inhibitor Development Service at CD BioGlyco

CD BioGlyco has a dedicated research team for the development of Glycosylation Inhibitors. N-Glycosylation is a type of glycosylation modification. It is involved in some processes including cell migration, differentiation, substance transport, transmembrane signaling, etc. The complexity and diversity of N-glycan structure may contain a great deal of biological information. It also correlates with the development of diseases. Therefore, the development of an N-Glycosylation Inhibitor is of greater significance. We provide inhibitor development services based on N-glycan-protein interaction.

• Metabolic inhibitors inhibit glycosylation by interfering with the metabolic or intracellular transport activity of common precursors of N-glycosylation. Some of these compounds act indirectly by inhibiting protein transport between the endoplasmic reticulum, Golgi, and trans-Golgi networks.
• Much of the initial work important to understanding glycan-protein interactions is gathered in studies of the binding sites of antibodies against specific blood group antigens and plant lectins. Plant lectins recognize glycans and their structures. The sugar-binding specificity it possesses gives it great potential for N-glycosylation inhibitor development. We screen for inhibitory plant lectins, anti-carbohydrate antibodies, etc., and compare their inhibitory effects.
• We resolve the crystal structure of the corresponding N-glycan-protein complex. Based on this, structure-based drug design approaches are used to obtain inhibitors capable of blocking N-glycan-protein interactions. We aim to screen or synthesize compounds that specifically block the N-glycan-protein interaction. The N-glycan-protein interaction is blocked without affecting other protein interactions.

Fig.1 Direction of inhibitor development based on N-glycan-protein interaction. (CD BioGlyco)

Publication

Technology: Computer-assisted screening

Journal: Molecules

IF:4.927

Published: 2021

Results: In this study, a compound library was established containing a variety of natural products, synthetic compounds, etc. CD147 is involved in the migration and invasion of cancer cells. In this study, computer-assisted screening of compounds that inhibit CD147 N-glycosylation from the established compound library was performed. A compound 72 was screened to act as an inhibitor of CD147 glycosylation. The hydrophobic interactions formed between three different glycosylation sites of CD147 and compound 72 enhanced the inhibitor-protein interaction. It completely blocks the conserved receptor sequences in CD147 N-glycosylation, thus providing an inhibitory effect.

Fig.2 Docking of compound 72 on the glycosylation sites. (Li, et al., 2020)

Applications

• We develop inhibitors based on N-glycan-protein interaction that is used to study the role of N-glycans in glycoprotein maturation, function, etc.
• The inhibitors we develop based on N-glycan-protein interaction are used to study disease mechanisms.
• The inhibitors we develop based on N-glycan-protein interaction are used to study immunomodulatory mechanisms.

Advantages

• We screen compounds in high throughput, which greatly reduces the time for inhibitor development.
• We have extensive experience in N-glycosylation research and inhibitor development, which ensures good inhibition and accuracy of results.
• Our development of inhibitors based on N-glycan-protein interaction provides an alternative approach to studying glycosylation in cells, tissues, etc., avoiding some of the problems encountered in studies through mutants.

CD BioGlyco has a complete and systematic N-glycosylation inhibitor development program. Our protocols are developed by experienced experts to provide the most professional service to our clients. If you are interested in our inhibitor development service based on N-glycan-protein interaction, please feel free to contact us. We will get back to you immediately.