Lacto-N-fucopentose III—a core oligosaccharide tool for glycobiological research CAS: 25541-09-7

Lacto-N-fucopentaose III (LNFP III) is a key structural unit in the complex between human lactooligosaccharides (HMOs) and various cell surface sugars. It is one of the core oligosaccharides of the fucosylated lactose series. Not only does it naturally exist in human milk, it is also the core skeleton of a variety of important biologically active sugar chains (such as Lewis blood group antigens, selectin ligands, etc.). As an indispensable high-purity standard and tool molecule in the field of glycobiology research and drug discovery, LNFP III is increasingly becoming the focus of cutting-edge directions such as infection immunity, tumor microenvironment, intestinal flora regulation, and vaccine design.

Chemical Information

Chemical name: Lacto-N-fucopentaose III

Common name: LNFP III

Chemical formula: C₃₂H₅₅NO₂₅

Molecular weight: 853.77 g/mol

CAS number: 25541-09-7

Structural features

LNFP III is a pentasaccharide composed of a lactose core connected to N-acetyllactosaminide through a β1-3 bond, and fucose modified at a specific position. Its structure can be briefly expressed as:

Galβ1-4GlcNAcβ1-3Galβ1-4Glc + α1-3Fuc (fucose is attached to the terminal Gal).

The uniqueness of this structure is:

Precise fucose positioning: α1-3 linked fucose modification gives it specific biorecognition function, making it a potential ligand for a variety of lectin receptors (such as DC-SIGN, selectins) and microbial adhesion proteins.

Core lactose-N-series skeleton: As a representative of type I lactose series oligosaccharides, its structure is highly similar to the carbohydrate antigens on the surface of various epithelial cells and immune cells. It is an ideal model molecule for studying host-pathogen interactions and cell signal transduction.

Good water solubility and stability: Under high purity, LNFP III is stable in aqueous solutions and is suitable for cell experiments, biochemical analysis and in vitro binding studies.

Main applications and advantages

1. Probes for the study of carbohydrate immunology and infection mechanism

Pathogen recognition research: Many viruses (such as HIV, influenza virus), bacteria and parasites use fucosylated oligosaccharides on the surface of host cells as invasion targets. LNFP III can be used as a key ligand to study the binding specificity and inhibition strategies of pathogen adhesion proteins (such as bacterial lectins).

Exploration of immunomodulatory functions: Human milk oligosaccharides can regulate infant immunity by simulating host cell surface sugar chains. As an important member, LNFP III is an ideal tool for studying the signaling pathways of C-type lectin receptors (such as DC-SIGN) on the surface of immune cells such as dendritic cells and macrophages, helping to reveal new mechanisms of innate immune recognition.

2. An important tool for tumor glycobiology and target discovery

Tumor-associated carbohydrate antigen simulation: Lewis X/a and other antigens are overexpressed or abnormally fucosylated on the surface of many tumor cells, and their structures are homologous or derived from LNFP III. Using high-purity LNFP III can help:

Screen or validate antibodies, chimeric antigen receptors (CARs), or small molecule inhibitors against tumor glycans.

Study the selectin-mediated tumor cell migration and metastasis process.

Tumor microenvironment regulation: Cell surface lectins such as tumor-associated macrophages (TAMs) can affect immune escape by recognizing fucosylated structures. LNFP III provides a clear molecular tool for exploring such interactions.

3. Standard materials for intestinal flora and microecology research

Prebiotic effect research: As an important component of human milk oligosaccharides, LNFP III can be selectively utilized by specific probiotics (such as bifidobacteria) to promote the colonization of beneficial bacteria. In in vitro culture or animal models, it can be used to study the regulatory effects of oligosaccharides on bacterial flora structure, short-chain fatty acid production, and intestinal barrier function.

Anti-pathogen colonization: LNFP III can competitively bind to the adhesins of intestinal pathogens (such as Escherichia coli and Helicobacter pylori) and block their binding to the intestinal epithelium. It is one of the candidate molecules for the development of "anti-adhesion" therapy.

4. Candidate molecules or vectors for drug and vaccine development

Vaccine design: Coupling LNFP III or its derivatives with carrier proteins can prepare glycoconjugate vaccines against specific pathogens (such as HIV, Mycobacterium tuberculosis) and induce the production of targeted antibodies.

Targeted delivery system: Utilizing the affinity of LNFP III for specific lectin receptors, it can be modified on the surface of liposomes or nanoparticles to achieve targeted delivery of drugs or genes to specific immune cells (such as dendritic cells).

Diagnostic reagent development: As a standard antigen, used to develop autoantibodies against fucosylated oligosaccharides in serum (such as in certain infections or autoimmune diseases), or used to optimize glycochip detection technology.

5. Core reagents for basic research and industrial production

Substrate for enzymatic analysis: As a specific substrate for fucosyltransferase and glycoside hydrolase, it is used for enzyme activity determination, inhibitor screening and catalytic mechanism research.

Analysis and detection standard: In HMOs detection and glycoprotein sugar chain analysis, LNFP III is a crucial qualitative and quantitative standard in HPLC, LC-MS, CE and other methods to ensure the accuracy and comparability of analysis results.

Biosynthesis and synthetic biology: As a target product, it guides enzymatic synthesis or the construction and optimization of microbial cell factories, and promotes the green large-scale production of functional oligosaccharides.

Conclusion

Lacto-N-fucopentose III is much more than a simple sugar molecule. It is a key bridge connecting glycochemistry and life sciences, and a molecular key to deciphering intercellular communication, immune recognition and microbial interactions. From the exploration of basic mechanisms to the development of new therapies, from intestinal health to tumor immunity, the potential of LNFP III is being continuously explored.