Use of human-milk fucosyltransferase in the chemoenzymic synthesis of analogues of the sialyl Lewis and sialyl Lewis tetrasaccharides modified at the C-2 position of the reducing unit

Nikrad, P. V.; Kashem, Mohammed A.; Wlasichuk, Kenneth B.; Alton, Gordon; Venot, André

doi:10.1016/0008-6215(93)84162-y

Cited by 29 publications

(4 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2-Chloro derivatives of Neu5Ac were used for the formation of a dimeric (2 → 8)-linked structure, , synthesis of 3-deoxy- d -glycero- d -galacto-2-nonulopyranosonic acid (KDN) glycosides, − synthesis of C - 63-65 and S -glycosides. ,,− Several other examples of the use of 2-chloro derivatives of Neu5Ac in the oligosaccharide synthesis have been reported. ,,,− …”

Section: 2-chloro Derivativesmentioning

confidence: 99%

Recent Advances in O-Sialylation

2000

View full text Add to dashboard Cite

Section: 2-chloro Derivativesmentioning

confidence: 99%

Recent Advances in O-Sialylation

2000

View full text Add to dashboard Cite

“…Salmonella typhimurium LT2 sialidase)-catalyzed transglycosylation reaction using pnitrophenyl α-N-acetylneuraminide (Neu5AcαpNP) as the glycosyl donor and Le a trisaccharide as the acceptor was reported but with poor glycosylation yields [25]. All reported glycosyltransferase-catalyzed chemoenzymatic synthesis of sLe a antigens were carried out using recombinant mammalian enzymes or human milk enzymes including human α1-4-fucosyltransferase (FucT III) [26,27] or human milk [28,29] α1-3/4fucosyltransferase, rat liver [22,23,26] or porcine submaxillary [28] α2-3-sialyltransferase, and/or human β1-3galactosyltransferase [26]. In general, the reactions were carried out by sialyltransferase-catalyzed sialylation of β1-3-linked galactosides followed by fucosylation in the last step [23].…”

Section: Introductionmentioning

confidence: 99%

Facile chemoenzymatic synthesis of Lewis a (Lea) antigen in gram-scale and sialyl Lewis a (sLea) antigens containing diverse sialic acid forms

Tasnima

Yan

et al. 2019

Carbohydrate Research

View full text Add to dashboard Cite

An efficient streamlined chemoenzymatic approach has been developed for gram-scale synthesis of Lewis a angtigen (Le a βProN 3 ) and a library of sialyl Lewis a antigens (sLe a βProN 3 ) containing different sialic acid forms. Intially, commercially available inexpensive N-acetylglucosamine (GlcNAc) was converted to its N′-glycosyl p-toluenesulfonohydrazide in one step. Followed by chemical glycosylation, GlcNAcβProN 3 was synthesized using this protecting group-free method in high yield (82%). Sequential one-pot multienzyme (OPME) β1-3-galactosylation of GlcNAcβProN 3 followed by OPME α1-4-fucosylation reactions produced target Le a βProN 3 in gram-scale. Structurally diverse sialic acid forms was successfully introduced using a OPME sialylation reaction containing a CMP-sialic acid synthetase and Pasteurella multocida α2-3sialyltransferase 1 (PmST1) mutant PmST1 M144D with or without a sialic acid aldolase to form sLe a βProN 3 containing naturally occurring or non-natural sialic acid forms in preparative scales.

show abstract

“…A chemically synthesized trisaccharide with a reducing end block was also suitable for this transformation [103,104]. This strategy was also applied to the synthesis of sLeX analogs bearing N-modifications [105]. In 1992, Ichikawa et al [106] reported the enzymatic total synthesis of sLeX from monosaccharides.…”

Section: Enzymatic Synthesismentioning

confidence: 99%

Essential functions, syntheses and detection of sialyl Lewis X on glycoproteins

Chen

2023

Explor Drug Sci

View full text Add to dashboard Cite

It is widely acknowledged that sialyl Lewis X (sLeX), the composition and linkage of which are N-acetylneuraminic acid (Neu5Ac) α2-3 galactose (Gal) β1-4 [fucose (Fuc) α1-3] N-acetylglucosamine, is usually attached to the cell surface. It presents as a terminal structure on either glycoproteins or glycolipids and has been demonstrated to be related to various biological processes, such as fertilization and selectin binding. Due to the vital role of sLeX, its synthesis as well as its determination approaches have attracted considerable attention from many researchers. In this review, the focus is sLeX on glycoproteins. The biological importance of sLeX in fertilization and development, immunity, cancers, and other aspects will be first introduced. Then the chemical and enzymatic synthesis of sLeX including the contributions from more than 15 international research groups will be described, followed by a brief view of the sLeX detection focusing on monosaccharides and linkages. This review is valuable for those readers who are interested in the chemistry and biology of sLeX.

show abstract

Use of human-milk fucosyltransferase in the chemoenzymic synthesis of analogues of the sialyl Lewis and sialyl Lewis tetrasaccharides modified at the C-2 position of the reducing unit

Cited by 29 publications

References 29 publications

Recent Advances in O-Sialylation

Recent Advances in O-Sialylation

Facile chemoenzymatic synthesis of Lewis a (Lea) antigen in gram-scale and sialyl Lewis a (sLea) antigens containing diverse sialic acid forms

Essential functions, syntheses and detection of sialyl Lewis X on glycoproteins

Contact Info

Product

Resources

About