Synthetic trisaccharides reveal discrimination of<i>endo</i>-glycosidic linkages by<i>exo</i>-acting α-1,2-mannosidases in the endoplasmic reticulum

Nitta, Kyohei; Kuribara, Taiki; Totani, Kiichiro

doi:10.1039/d1ob00428j

Cited by 5 publications

(4 citation statements)

References 38 publications

(39 reference statements)

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“…The reaction in this solvent was performed at a warmer temperature, resulting in 15 with complete α-selectivity, similar to a previous study comparing the solvent effect between toluene and dichloromethane. 17 We postulate toluene enhanced the neighboring group participation by both the low polarity and noncoordination to the cations. Next, we substituted MS4A with MS AW-300, another molecular sieve with a 4 Å pore size (entry 4), to examine the factors influencing the moderate yield despite complete consumption of the acceptor.…”

Section: ■ Results and Discussionmentioning

confidence: 85%

“…Therefore, we used toluene as a solvent, which has a low polarity (entry 3). The reaction in this solvent was performed at a warmer temperature, resulting in 15 with complete α-selectivity, similar to a previous study comparing the solvent effect between toluene and dichloromethane . We postulate toluene enhanced the neighboring group participation by both the low polarity and noncoordination to the cations.…”

Section: Resultsmentioning

confidence: 99%

“…The Man 9 GlcNAc 2 ( M9 ) glycan on the protein surface typically acts as a folding checkpoint (Figure b). The removal of Man residues by endoplasmic reticulum (ER) α1,2-mannosidases defines whether the glycoprotein is secreted or degraded . The Man 8B GlcNAc 2 ( M8B ) glycan functions as a secretion signal, whereas Man 8C GlcNAc 2 ( M8C ) and further trimmed Man 7 GlcNAc 2 ( M7 ) glycans act as degradation signals .…”

Section: Introductionmentioning

confidence: 99%

“…The removal of Man residues by endoplasmic reticulum (ER) α1,2mannosidases defines whether the glycoprotein is secreted or degraded. 17 The Man 8B GlcNAc 2 (M8B) glycan functions as a secretion signal, whereas Man 8C GlcNAc 2 (M8C) and further trimmed Man 7 GlcNAc 2 (M7) glycans act as degradation signals. 18 Glucosidase II, an enzyme related to glycoprotein quality control, has been reported to exhibit differences in r e a c t i v i t y b e t w e e n G l c 1 M a n 8 B G l c N A c 2 a n d Glc 1 Man 8C GlcNAc 2 , highlighting the significance of the Band C-arms in high-mannose-type glycan isoform.…”

Section: ■ Introductionmentioning

confidence: 99%

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Multisite Partial Glycosylation Approach for Preparation of Biologically Relevant Oligomannosyl Branches Contribute to Lectin Affinity Analysis

Usui,

Koizumi,

Nitta

et al. 2023

J. Org. Chem.

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High-mannose-type glycans play essential biological roles, e.g., immune response and glycoprotein quality control, and preparing a series of oligomannosyl branches of high-mannose-type glycans is critical for biological studies. However, obtaining sufficient amounts of the various oligomannosyl branches is challenging. In this study, we demonstrated a partial glycosylation strategy for the single-step synthesis of various biologically relevant oligomannosyl-branched structures. First, Manα1-6(Manα1-3)Man-type oligomannosyl branch was synthesized via double glycosylation from a 3,6-di-OH mannosyl acceptor and fluorinated mannosyl donor with perfect α-selectivity. Subsequent partial glycosylation by reducing the equivalent of the mannosyl donor enabled to obtain biologically relevant Manα1-2Manα1-6(Manα1-2Manα1-3)Man, Manα1-6(Manα1-2Manα1-3)Man, Manα1-2Manα1-6(Manα1-3)Man, and Manα1-6(Manα1-3)Man in one-pot. Each oligomannosyl branch could be easily purified by liquid chromatography. The resulting structural isomers were identified by 2D-HMBC NMR. A systematic lectin affinity assay using the prepared oligomannosyl branches showed different specificities for the Galanthus nivalis lectin between structural isomers of the oligomannosyl branches with the same number of mannose residues..

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Section: ■ Results and Discussionmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Multisite Partial Glycosylation Approach for Preparation of Biologically Relevant Oligomannosyl Branches Contribute to Lectin Affinity Analysis

Usui,

Koizumi,

Nitta

et al. 2023

J. Org. Chem.

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Synthesis of a fluorescent probe for measuring the activity of endo-β-N-acetylglucosaminidases recognizing hybrid-type N-glycans

Ishii,

Inoue,

Sano

et al. 2024

Bioorganic & Medicinal Chemistry

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Catalytic Thioglycoside Activation with Diazo-Derived Copper Carbenes

Singh,

Chaudhary,

Sharma

2024

Molecules

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Traditional glycosylation methods using thioglycosides often require harsh conditions or expensive metal catalysts. This study presents a more sustainable alternative by employing copper, an earth-abundant catalyst. We developed diazo-based thioglycoside donors that, through copper catalysis, undergo intramolecular activation to form glycosyl sulfonium ions, leading to the generation of oxocarbenium ions. This versatile approach efficiently accommodates a variety of O-nucleophiles, including primary, secondary, and tertiary, as well as complex bioactive molecules. It is compatible with various glycosyl donors and protecting groups, including superarmed, armed, and disarmed systems. Notably, the methodology operates orthogonally to traditional thioglycoside and alkyne donors and has been successfully applied to the orthogonal iterative synthesis of trisaccharides. Mechanistic insights were gained by studying the electronic effects of electron-donating (OMe) and electron-withdrawing (NO2) groups on the donors, offering a valuable understanding of the intramolecular reaction pathway.

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Synthetic trisaccharides reveal discrimination ofendo-glycosidic linkages byexo-acting α-1,2-mannosidases in the endoplasmic reticulum

Abstract: Tri-antennary Man9GlcNAc2 glycan on the surface of endoplasmic reticulum (ER) glycoproteins functions as a glycoprotein secretion or degradation signal after regioselective cleavage of the terminal α-1,2-mannose residue of each branch....

Cited by 5 publications

References 38 publications

Multisite Partial Glycosylation Approach for Preparation of Biologically Relevant Oligomannosyl Branches Contribute to Lectin Affinity Analysis

Multisite Partial Glycosylation Approach for Preparation of Biologically Relevant Oligomannosyl Branches Contribute to Lectin Affinity Analysis

Synthesis of a fluorescent probe for measuring the activity of endo-β-N-acetylglucosaminidases recognizing hybrid-type N-glycans

Catalytic Thioglycoside Activation with Diazo-Derived Copper Carbenes

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