Lacto-N-difucohexaose I (LNDFH I) Production Service

Lacto-N-difucohexaose I (LNDFH I) Production Service

LNDFH I is a typical HMO with a Lewis b structure, which would be a promising substance to research as an H. pylori adhesin. CD BioGlyco provides LNDFH I production service for clients to meet their needs.

Production Methods of LNDFH I

The main components of human milk oligosaccharides (HMOs) are 2ʹ-fucosyllactose (2FL), lacto-N-tetraose (LNT), lacto-N-fucopentaose I, and lacto-N-difucohexaose I (LNDFH I), all but 2FL being in the LNT series. Oligosaccharides of the LNT series are referred to as type I oligosaccharides because they have a lacto-N-biose I (LNB) backbone not found in other mammals.

The structure of LNDFH I.Fig.1 The structure of LNDFH I. (Figueroa-Lozano & de Vos, 2018)

Enzymatic Synthesis is a potent method for producing LNDFH I. Bovine blood is initially used to partially isolate 1,3-N-acetylglucosaminyltransferase (-1,3-GnT). By joining d-GlcNAc to the d-galactose residue, this enzyme preparation transforms lactose into lacto-N-triose II. Afterward, ortho-nitrophenyl-d-galactopyranoside, which acts as a donor, is transglycosylated by recombinant 1,3-galactosidase from Bacillus circulans to produce LNT. The l-fucose is then bound to the d-galactose residue of LNT through a -1,2-linkage using recombinant human fucosyltransferase I (FUT1) produced in a baculovirus system. Then, GDP-l-fucose and commercial fucosyltransferase III are incubated with the resultant pentasaccharide to bind l-fucose to the d-GlcNAc residue of LNT with a 1,4-linkage (FUT3). After purification with activated carbon column chromatography, LNDFH I is created.

Enzymatic Synthesis of LNDFH I.Fig.2 Enzymatic Synthesis of LNDFH I. (Miyazaki, et al., 2010)

LNDFH I Production Service at CD BioGlyco

It is believed that LNDFH I, a typical HMO with a Lewis b structure, would be a promising substance to research as an H. pylori adhesin. On a preparative scale, this hexasaccharide has already been chemically produced. Using the glycan assembly approach, the Chemical Synthesis of LNDFH I has also been accomplished. However, chemical synthesis is time-consuming and labor-intensive since it requires many steps of synthetic manipulations. Although glycosyltransferases are difficult to come by and sugar nucleotides are expensive, Enzymatic Synthesis employing these enzymes is a potent method for creating oligosaccharides with regio- and stereo-selectivity.

Based on that, CD BioGlyco provides production services with different production methods according to the client's needs and we have the ability to customize different scales and grades of LNDFH I synthesis. For giving our clients the greatest possible assistance, the HMO Analysis Platform at CD BioGlyco will also be an excellent choice for clients to study HMO.

Advantages of Us

  • We have an advanced and completed platform to provide synthesis and analysis services for LNDFH I.
  • We synthesize different scales and grades of LNDFH I according to the client's needs.
  • We have great scientists and an outstanding service team to help our clients to study the field of LNDFH I.
  • We have the ability to process different production programs for our clients and it is useful for clients to choose the best suitable production method.

CD BioGlyco has a powerful and advanced synthesis platform for high-quality synthesis services. We have the ability to customize different scales and grades of LNDFH I synthesis according to the client's needs, and we are committed to being a first-choice assistant for our clients in the field of HMO research. If you are interested in the production service for LNDFH I, please feel free to contact us for more detailed information.

References:

  1. Figueroa-Lozano, S.; and de Vos, P. Relationship between oligosaccharides and glycoconjugates content in human milk and the development of the Gut Barrier. Comprehensive Reviews in Food Science and Food Safety. 2018, 18(1): 121–139.
  2. Miyazaki, T.; et al. Enzymatic synthesis of lacto-N-difucohexaose I which binds to helicobacter pylori. Methods in Enzymology. 2010, 511–524.
This service is for Research Use Only, not intended for any clinical use.

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