Mannosyltransferase Inhibitor Development Service

Mannosyltransferase Inhibitor Development Service

Mannosyltransferase Inhibitor Development Service at CD BioGlyco

Mannosyltransferase is one of the enzymes involved in the synthesis of glycosylphosphatidylinositol (GPI) anchor, which catalyzes the transfer of glucose to the mannose residue in the GPI structure. It mainly includes three types of enzymes.

  • α1-4-Mannosyltransferase (GPIMT-I): It is responsible for adding the first mannose residue to the precursor molecule of GPI, catalyzing the connection between UDP-mannose and the precursor structure of GPI, forming the primary structure of GPI.
  • α1-6-Mannosyltransferase (GPIMT-II): It progressively adds more mannose residues to the precursor of GPI. This process gradually expands the complexity of the GPI structure through a series of reactions.
  • α1-2-Mannosyltransferase (GPIMT-III): It is responsible for adding the last mannose residue in the synthesis of GPI.

The synergistic effect of these three enzymes ensures that GPI-anchored proteins are synthesized correctly so that they are positioned on the cell membrane. Based on this mechanism, CD BioGlyco provides specialized mannosyltransferase inhibitor development services, which help provide new strategies and approaches for the research of various diseases.

  • Diversified mannosyltransferase inhibitor development service

Our research team conducts basic structural research on mannosyltransferase through X-ray crystallography, nuclear magnetic resonance, and other techniques, they master the structure of mannosyltransferase as well as its substrate binding site and reaction mechanism, which is an important basis for the development of inhibitors. We offer a diverse approach to mannosyltransferase inhibitor development.

    • Substrate competitive inhibitors: CD BioGlyco designs molecules based on the substrate binding site of mannosyltransferase so that they compete with the substrate binding site. For example, 4-deoxy-GlcN-PI analogs are substrate-competitive inhibitors of GPIMT-I.
    • Mechanism-oriented inhibitors: CD BioGlyco is familiar with the reaction mechanism of mannosyltransferase, has found the key links of this mechanism, and develops mannosyltransferase inhibitors by interfering with the key links.
    • High-throughput screening: CD BioGlyco also utilizes high-throughput screening technology to rapidly screen large-scale compound libraries to find candidate compounds with inhibitory activity against specific mannosyltransferase.
  • Chemical synthesis service

CD BioGlyco further chemically modifies and optimizes the structure of the candidate mannosyltransferase inhibitors obtained through preliminary screening to enhance their selectivity, affinity, and pharmacokinetic properties. We perform efficient synthesis, purification, and characterization based on optimized inhibitor structures.

  • Activity assessment service

CD BioGlyco provides skilled activity assessment services such as enzyme activity measurement, cell experiments, and animal model research. Through in vitro and in vivo experiments, we evaluate the impact of inhibitors on the activity of the target mannosyltransferase and determine its efficacy and mechanism.

Fig.1 Mannosyltransferase inhibitor development service. (CD BioGlyco)Fig.1 Mannosyltransferase inhibitor development service. (CD BioGlyco)


Technology: Thin-layer chromatography

Journal: The EMBO Journal

IF: 13.783

Published: 1997

Results: The authors used a screening approach to find natural compound inhibitors of GPI-anchored synthesis in yeast and identified YW3548, a terpene lactone that blocked the incorporation of a third mannose into the intermediate structure of GPI. The authors analyzed the effect of YW3548 on in vitro GPI synthesis in S. cerevisiae (A), P. falciparum (B), and T. brucei (C). The results indicated that YW3548 blocked GPI synthesis in yeast and mammalian cells, but not in protozoa, indicating that there were significant interspecies differences in GPI synthesis.

Fig.2 The role of YW3548 in protozoan systems. (Sütterlin, et al., 1997)Fig.2 The role of YW3548 in protozoan systems. (Sütterlin, et al., 1997)


  • Antifungal research: Mannosyltransferase plays a key role in fungal cell wall synthesis. By developing inhibitors of mannosyltransferase, the synthesis process of fungal cell walls is interfered with, thereby preventing fungal growth and spread, which has potential applications for studying fungal infections such as Candida and Aspergillus infections.
  • Anti-parasitic research: Some parasites rely on mannosyltransferase to synthesize the glycosylation structure of their surface membrane. Inhibiting mannosyltransferase destroys the cell wall structure of parasites and affects their survival and development, thus providing new strategies for anti-parasitic research.
  • Anti-cancer research: Glycosylation modifications on the surface of tumor cells are closely related to their invasion and metastasis capabilities. By interfering with glycosylation modification mediated by mannosyltransferase, the metastasis and invasion of tumor cells are inhibited.


  • Multidisciplinary team: CD BioGlyco has established an interdisciplinary team of experts, including medicinal chemists, structural biologists, computational chemists, and pharmacodynamics experts, who collaborate on mannosyltransferase inhibitor development projects from multiple perspectives.
  • Comprehensive Inhibitor Development Solutions: CD BioGlyco has a wide range of technology solutions, including molecular simulation, high-throughput screening, structure-activity relationship (SAR) analysis, pharmacokinetic evaluation, etc., to support a full range of mannosyltransferase inhibitor development.
  • Strict quality control: CD BioGlyco has established a strict quality management system to ensure the accuracy, repeatability, and reliability of the mannosyltransferase inhibitor development process and results.

CD BioGlyco provides high-quality and efficient mannosyltransferase inhibitor development service, and we have effective project management capabilities to ensure results are delivered on time and meet client's requirements. Please feel free to contact us if you would like to acquire detailed development information.


  1. Sütterlin, C.; et al. Identification of a species-specific inhibitor of glycosylphosphatidylinositol synthesis. The EMBO Journal. 1997, 16(21): 6374-6383.
  2. Smith, T.K. Inhibitors of GPI biosynthesis. The Enzymes. 2009, 26: 247-267.
This service is for Research Use Only, not intended for any clinical use.

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