Synthesis of disaccharide glycosyl donors suitable for introduction of the β-d-Galp-(1 → 3)-α- and -β-d-Gal pNAc groups

Wilstermann, Michael; Magnusson, Göran

doi:10.1016/0008-6215(95)00026-p

Cited by 27 publications

(21 citation statements)

References 17 publications

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“…[18] Glycosylation of the threoninyl a-glycoside 7 as an acceptor with the known thioglycoside donor 8 in the presence of N-iodosuccinimide (NIS) and TfOH gave the desired disaccharide 9 in 93 % yield. [21] A large amount of TfOH (0.4 equiv) was used in order to avoid formation of the ortho-ester. In the last step, the azido moiety and the benzyl ester of 9 were hydrogenated with 5 % Pd/C under H 2 to provide the amino glycoside.…”

Section: Resultsmentioning

confidence: 99%

Facile Solid-Phase Synthesis of an Antifreeze Glycoprotein

Tseng¹,

Jiaang²,

Chang³

et al. 2001

Chem. Eur. J.

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The antifreeze glycoproteins (AFGPs) 1 are composed of a repeating tripeptide unit (Ala-Thr-Ala) in which the threonine residue is glycosylated with the disaccharide beta-D-Gal-(1-->3)-alpha-D-GalNAc. A new procedure for synthesizing AFGPs using Fmoc-(Ac4-beta-D-Gal-(1-->3)-benzylidene- alpha-D-GalNAc)Thr-OH (10) as a building block has been developed. Total synthesis of the AFGPs (n = 4, 8) in overall yields of 61% and 33 %, respectively, has demonstrated the usefulness of the method. The synthetic AFGPs 1 (n = 4, 8) showed a similar conformation to the native AFGPs in their circular dichroism spectra.

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Section: Resultsmentioning

confidence: 99%

Facile Solid-Phase Synthesis of an Antifreeze Glycoprotein

Tseng¹,

Jiaang²,

Chang³

et al. 2001

Chem. Eur. J.

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“…The mucin-1 tandem repeat peptides were synthesized by stepwise solid-phase peptide synthesis using the Fmoc strategy, and starting with a preloaded Fmoc-alanine trityl resin (8,10 or 13 mmol scale/peptide). The synthesis employed the protected core 1 (13), core 2 (19) and core 3 (23) threonine amino acid building blocks, which were preactivated manually using 1.5 or 2 equivalents and activated with HATU/HOAt, while the other Fmoc amino acids were coupled automatically on a Multisyntech peptide synthesizer using 8 equiv of the amino acid and the HBTU/HOBt reagents. Fmoc deprotection was performed according to standard conditions, 20 % piperidine in DMF.…”

Section: General Methods Glycopeptide Synthesismentioning

confidence: 99%

“…CH 3 -(Ac)),18.7 ppm (T g ). HRMS (ESI) (pos): m/z calcd for C 73 H 96 N 3 O 36 + : 1590.5774 [M + H] + ; found: 1590.5772. tetra-O-acetyl-b-d-galactopyranosyl)-b-d-glucopyranosyl]-b-d-galactopyranosyl}-a-d-galactopyranosyl)-lthreonine (Fmoc-Thr(bAc 4 Gal-(1!3)-bAc 2 GlcNAc-(1!3)-Ac 3 Gal-(1!3)-aAc 2 GalNAc)-OH)(19): To a solution of compound 18 (1.20 g, 0.75 mmol) in dichloromethane (5 mL) and anisole (0.5 mL) was added trifluoroacetic acid(15 mL) and the reaction mixture was stirred for 90 min. The solvent was removed by co-evaporation with toluene.…”

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confidence: 99%

A Convergent Strategy for the Synthesis of Type‐1 Elongated Mucin Cores 1–3 and the Corresponding Glycopeptides

Pett

Westerlind

2014

Chemistry A European J

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Mucins are a class of highly O-glycosylated proteins found on the surface of cells in epithelial tissues. O-Glycosylation is crucial for the functionality of mucins and changes therein can have severe consequences for an organism. With that in mind, the elucidation of interactions of carbohydrate binding proteins with mucins, whether in morbidly altered or unaltered conditions, continue to shed light on mechanisms involved in diseases like chronic inflammations and cancer. Despite the known importance of type-1 and type-2 elongated mucin cores 1-4 in glycobiology, the corresponding type-1 structures are much less well studied. Here, the first chemical synthesis of extended mucin type-1 O-glycan core 1-3 amino acid structures based on a convergent approach is presented. By utilizing differentiation in acceptor reactivity, shared early stage Tn- and T-acceptor intermediates were elongated with a common type-1 [β-D-Gal-1,3-β-D-GlcNAc] disaccharide, which allows for straightforward preparation of diverse glycosylated amino acids carrying the type-1 mucin core 1-3 saccharides. The obtained glycosylated 9-fluorenylmethoxycarbonyl (Fmoc)-protected amino acid building blocks were employed in synthesis of type-1 mucin glycopeptides, which are useful in biological applications.

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“…Given their significances, both chemical 10 and enzymatic strategies 11 were developed for the synthesis of these glycans. Previously, we cloned a novel D-galactosyl-β1–3- N -acetyl-D-hexosamine phosphorylase from Bifidobacterium infantis (BiGalHexNAcP), and developed a highly efficient one-pot two-enzyme system for rapid preparation of GNB and lacto- N -biose (LNB, Galβ1–3GlcNAc) as well as their derivatives.…”

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confidence: 99%

Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms

Liu

et al. 2015

Chem. Commun.

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Galacto-N-biose (GNB) derivatives were efficiently synthesized from galactose derivatives via a one-pot two-enzyme system containing two promiscuous enzymes from Bifidobacterium infantis: a galactokinase (BiGalK) and a D-galactosyl-β1–3-N-acetyl-D-hexosamine phosphorylase (BiGalHexNAcP). Mono-sialyl and di-sialyl galacto-N-biose derivatives were then prepared using a one-pot two-enzyme system containing a CMP-sialic acid synthetase and an α2–3-sialyltransferase or an α2–6-sialyltransferase.

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Synthesis of disaccharide glycosyl donors suitable for introduction of the β-d-Galp-(1 → 3)-α- and -β-d-Gal pNAc groups

Cited by 27 publications

References 17 publications

Facile Solid-Phase Synthesis of an Antifreeze Glycoprotein

Facile Solid-Phase Synthesis of an Antifreeze Glycoprotein

A Convergent Strategy for the Synthesis of Type‐1 Elongated Mucin Cores 1–3 and the Corresponding Glycopeptides

Efficient chemoenzymatic synthesis of novel galacto-N-biose derivatives and their sialylated forms

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