CAS: 173935-46-1— A key building block in glycopeptide synthesis and glycobiology research
Today, with the rapid development of glycochemistry and glycobiology, glycosylation modification, as one of the most extensive and important post-translational modifications in life processes, is increasingly becoming the focus of drug development and disease mechanism research. Fmoc-Ser(Ac₃Fucα)-OH is an Fmoc-protected serine derivative with a clear structure and easy operation. The serine side chain hydroxyl group is specifically connected to a fully acetylated α-configuration fucose (Fuc) group. This compound is a key building block for the chemical synthesis of structurally uniform and biologically relevant glycoglycopeptides, providing a powerful chemical tool for glycoprotein functional studies, carbohydrate vaccine development, and drug discovery based on carbohydrate structures.
Today, with the rapid development of glycochemistry and glycobiology, glycosylation modification, as one of the most extensive and important post-translational modifications in life processes, is increasingly becoming the focus of drug development and disease mechanism research. Fmoc-Ser(Ac₃Fucα)-OH is an Fmoc-protected serine derivative with a clear structure and easy operation. The serine side chain hydroxyl group is specifically connected to a fully acetylated α-configuration fucose (Fuc) group. This compound is a key building block for the chemical synthesis of structurally uniform and biologically relevant glycoglycopeptides, providing a powerful chemical tool for glycoprotein functional studies, carbohydrate vaccine development, and drug discovery based on carbohydrate structures.
Chemical Information
Chemical name: N-(9-fluorenemethoxycarbonyl)-O-[2,3,4-tri-O-acetyl-α-L-fucofuranosyl]-L-serine
Common name: Fmoc-serine (2,3,4-tri-O-acetyl-α-L-fucoside)
Chemical formula: C₃₀H₃₃NO₁₂
Molecular weight: 599.59 g/mol
CAS number: 173935-46-1
Category: Glycopeptides
Structural features
The design of Fmoc-Ser(Ac₃Fucα)-OH has both synthetic applicability and biological relevance:
Fmoc protection strategy compatibility: Its α-amino group is protected by 9-fluorenylmethoxycarbonyl (Fmoc), which allows it to be perfectly integrated into the standard Fmoc solid-phase peptide synthesis process and facilitates the efficient assembly of glycopeptide sequences through automated synthesizers.
Pre-protection and activation of sugar groups: The hydroxyl groups on fucose are all protected by acetyl groups. This not only improves the stability of the building blocks during the synthesis process and prevents unnecessary side reactions, but also creates conditions for the subsequent selective removal of acetyl groups through mild alkali treatment after the peptide chain assembly is completed, exposing the free fucose hydroxyl groups.
Specific glycosidic bond configuration: Fucose is precisely connected to the hydroxyl group of serine with α-glycosidic bond. α-linked fucose, especially when present at the N-linked or O-linked glycan termini of glycoproteins, plays a critical role in numerous cellular recognition, signaling, and immunomodulatory processes.
Main applications and value
Synthesis of glycopeptides and glycoprotein mimetics
This compound is an ideal starting material for the chemical synthesis of glycopeptides, glycoprotein fragments or mimetics containing O-linked fucose modifications. Through solid-phase peptide synthesis technology, researchers can introduce this precisely modified serine unit into specific positions of the polypeptide chain in a targeted and quantitative manner, thereby obtaining structurally uniform glycopeptides for studying the precise effects of glycosylation on the structure, stability, activity, and interaction of peptides/proteins.
Basic research tools on glycobiology
Research on enzymatic substrates and inhibitors: The synthesized specific glycopeptides can be used as substrates to study the activity, specificity and kinetics of fucosyltransferase or fucosidase, or to screen and evaluate related enzyme inhibitors.
Molecular recognition and interaction research: Fucose is a key recognition ligand for many lectins (such as selectins, DC-SIGN, etc.). Glycopeptides synthesized using this building block can be used to explore the molecular mechanisms, affinity and structural basis of protein-sugar interactions, which are crucial for understanding processes such as inflammation, cancer metastasis and pathogen infection.
Development of carbohydrate vaccines and therapeutic drugs
Designing glycopeptide vaccines based on tumor-related or pathogen-specific glycoantigens (which often contain fucose modifications) is one of the frontiers of immunotherapy. Fmoc-Ser(Ac₃Fucα)-OH provides a reliable chemical means to construct such immunogens with clear structures and carrying specific sugar epitopes. In addition, glycopeptides or analogs containing fucose modifications may themselves serve as therapeutic candidate molecules for intervening in abnormal cell adhesion or signaling pathways.
Conclusion
Fmoc-Ser(Ac₃Fucα)-OH is not only a glycopeptide synthesis building block, but also a bridge connecting synthetic chemistry and glycolife science. Its convenience in synthesis and biological relevance in structure make it possible to deeply analyze the biological function of fucosylation, an important modification, and promote innovative therapies based on sugar structure.
The above information is provided by the editor of KASONS and is for scientific research only.