ST3Gal Inhibitor Development Service
ST3Gal Inhibitor Development Service at CD BioGlyco
CD BioGlyco has specifically constructed the appropriate compound libraries to meet Glycosylation Inhibitor Development needs. Sialylation is a glycosylation modification process catalyzed by one or more sialyltransferases and sialidases. Sialyltransferases are categorized into four families based on the different positions at which they attach sialic acid residues to the sugar chain. ST3Gal is a type of sialyltransferase. Based on the key role of sialic acid modification in cellular life activities, its correlation with diseases, etc., the Development of Sialylation Inhibitors is very necessary. We provide ST3Gal inhibitor development services to meet the various research needs of our clients regarding sialylation.
Fig.1 Classes of ST3Gal inhibitor development. (CD BioGlyco)
Donor analogs and transition state analogs are effective inhibitors of glycosyltransferases. We screen fluorinated analogs, peracetylated analogs, etc., as donor analogs and transition state analogs of sialylation. They competitively bind to ST3Gal and thus inhibit the sialylation process.
CMP-Sialic acid participates in the glycosylation modification process as a sialic acid donor. CMP-Sialic acid analogs are found to be effective sialyltransferase inhibitors. Several CMP-sialic acid analogs with inhibitory activity against ST3Gal have been developed. Based on the reported strategies for inhibitor development, we screen donor analogs, dual-substrate analogs, etc., with broad inhibitory activity against ST3Gal.
We inhibit the catalytic activity of ST3Gal by using modified lactosamine and lactose which increase the acceptor specificity and decrease the donor reactivity.
To improve screening capability and efficiency, we construct specialized compound libraries. We aim to screen compounds with reliable quality, inhibitory activity, and selectivity.
Publication
Technology: High throughput quantitative screening based on matrix-assisted Laser desorption and Ionization time-of-flight mass spectrometry (MALDI-TOFMS)
Journal: Journal of Medicinal Chemistry
IF:4.802
Published: 2010
Results: This study describes a method for selective screening of potent sialyltransferase inhibitors by high-throughput quantitative screening based on MALDI-TOFMS. Ultimately, from the constructed focused compound libraries constructed by 1,3-dipolar cycloaddition of the desired azidosugar nucleotides with various alkynes, the researchers screened for an inhibitor of α2,3-ST (ST3Gal III) with potent inhibitory activity (compound 15). The compound was tested to be a good donor substrate for α2,6-ST (ST6Gal I).
Fig.2 Inhibitory effect on ST3Gal III and ST6Gal of heterobifunctional molecule. (Hosoguchi, et al., 2010)
Applications of ST3Gal Inhibitor Development
- ST3Gal inhibitor development can pave the way for exploring the role of sialylated glycans in biology and disease mechanisms.
- ST3Gal inhibitor development offers the possibility of developing drugs for diseases associated with high expression of sialic acid and sialyltransferase.
- The developed ST3Gal inhibitors are used to probe carbohydrate-enzyme interactions.
Advantages of Us
- We ensure that our clients are provided with efficient inhibitors for their sialylation studies, guaranteeing them successful studies.
- We have carefully constructed compound libraries for sialylation inhibitor development and make adjustments as experiments progress.
- We screen compounds in high throughput.
CD BioGlyco is expanding the synthesis of structural analogs, structural derivatives, etc., around the discovered sialylation inhibitors. If you are interested in our services, please feel free to contact us to learn more about the ST3Gal inhibitor development process, compound libraries, and more. We look forward to providing satisfactory ST3Gal inhibitor development services for your research.
Reference
- Hosoguchi, K.; et al. An efficient approach to the discovery of potent inhibitors against glycosyltransferases. Journal of Medicinal Chemistry. 2010, 53(15): 5607-5619.
