Monofucose lactose-N-hexose III: the precise key to the sugar code of life CAS number: 96656-34-7

In the grand picture of life sciences, proteins and nucleic acids have long occupied the center stage of research. However, there is a class of molecules that, although they have complex structures and are unknown, regulate almost every important life process - they are glycans. Today, we solemnly introduce to you the top tools and key standards in the field of glycan research: monofucose lactose-N-hexose III. It is not only a chemical molecule, but also a precise key to unlocking core biological mechanisms such as cell communication, pathogen infection, and immune regulation.

Chemical Information

Chemical name/structural description: Monofucose lactose-N-hexose III (derived from human milk oligosaccharide structure)

Common name: Fucosyllacto-N-hexaose III, FLNH-III

Chemical formula: C₄₆H₇₈N₂O₃₅

Molecular weight: 1219.1 g/mol

CAS number: 96656-34-7

Appearance: White to off-white freeze-dried powder

Solubility: Easily soluble in water, dimethyl sulfoxide (DMSO)

Structural features: Nature’s exquisite “identification code”

Monofucose lactose-N-hexose III belongs to one of the core complex structures in the human milk oligosaccharide (HMO) family. The subtleties of its structure are:

Precise fucosylation positioning: This molecule has a fucose group attached to a specific position on the lacto-N-neohexaose backbone. This α1-3 or α1-4 linked fucosylation is the basis for the formation of key blood group epitopes (eg, Lewis X, Lewis A) and selectin ligand structures.

Three-dimensional space recognition code: Its branched hexasaccharide structure forms a unique epitope in space, which can be recognized with high specificity by specific lectins (such as DC-SIGN), selectins (such as E-selectin) and antibodies. This recognition is not a simple "lock and key", but a sophisticated "handshake" that determines inter-cell adhesion, signal transduction and immune response.

Main applications and core values

1. Revolutionary tool for infectious disease research

Many pathogens, including viruses (such as HIV, influenza virus), bacteria and parasites, initiate infection by recognizing specific glycan structures on the surface of host cells (such as the Lewis epitope contained in this molecule).

Mechanism decryption: FLNH-III is used as a competitive inhibitor or immobilized ligand to study the binding mechanism of pathogen adhesion proteins (such as viral hemagglutinin, bacterial lectin) and host cells to clarify the first step of infection.

Drug Development Target Validation: It is a key molecular probe for the development of new anti-infection therapies (such as glycan analog inhibitors, vaccine design), and is used to validate and screen drug candidates that can block this deadly "sugar recognition".

2. Research on immune regulation and tumor microenvironment

Glycans are an important component of immune checkpoints and profoundly regulate the occurrence and development of tumors.

Immune cell navigation: FLNH-III and similar structures are ligands of selectins (E-selectin, P-selectin), mediating the directional rolling and homing of leukocytes to inflammatory sites or lymph nodes. Studying its role can reveal the deep rules of immune cell trafficking.

Tumor immune evasion: Tumor cells often abnormally express specific fucosylated glycans (such as Sialyl Lewis X) on the surface to evade immune surveillance or promote metastasis. In-depth research using FLNH-III with a clear structure will help elucidate the glycobiological basis of tumor immune escape and provide ideas for a new generation of immunotherapy.

3. Standard reference materials for glycomics and biomarker analysis

Qualitative quantification of complex biological samples is a huge challenge in glycomic analysis based on mass spectrometry or liquid chromatography.

Gold standard for characterization and calibration: FLNH-III can be used as an absolute standard to establish retention time databases and calibration curves for analytical methods, and to accurately quantify the corresponding glycan structures in complex samples (such as serum, tissue extracts).

Disease marker discovery: By comparing changes in specific fucosylated glycan levels in healthy and disease states (such as cancer, inflammatory diseases), FLNH-III can be used as a reference to help discover new carbohydrate biomarkers with diagnostic or prognostic value.

4. Optimization factors for cell culture and regenerative medicine

Glycans profoundly affect stem cell self-renewal, differentiation, and cell-cell interactions.

Stem cell fate regulation: Adding such well-defined glycans or their derivatives to stem cell culture media may finely regulate the maintenance of pluripotency or differentiation into specific lineages (such as nerves and hematopoietic cells), providing a better in vitro culture system for regenerative medicine.

Organoids and tissue engineering: When constructing organoids or biological materials, introducing functional glycan signals can better simulate the microenvironment in the body and promote the construction of more realistic and functional three-dimensional tissue models.

Conclusion

Monofucose lactose-N-hexose III, behind this seemingly long name, carries the ancient language of life communication. Today, with the rapid development of precision medicine and biotechnology, an in-depth understanding of the functions of glycans has become the next scientific high ground to be fought for.

The above information is provided by the editor of KASONS and is for scientific research only.