Synthesis, conformational analysis and GalNAc–lectin interactions of a constrained C-glycoside analogue of the TN antigen

文献情報

出版日 2023-12-28

DOI 10.1039/D3NJ05184F

インパクトファクター 3.591

著者

Juliette Dourdan, Florian Rouzier, Thanh Thao Huynh, Sullivan Bricaud, Arnaud Nourry, Stéphane Guillarme

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要旨

Highly stereoselective 1,3-dipolar cycloaddition allowed the synthesis of the original stable TN antigen mimic presenting a constraint on the amino acid part. Two main conformations of the GalNAc moiety were detected by molecular modelling and NMR. A ligand/protein interaction study was performed by saturation transfer difference NMR analyses using two GalNAc-specific model lectins highlighting that the constrained C-glycoside analog was recognized by these proteins as well as the TN antigen derivative.

掲載誌

New Journal of Chemistry

CiteScore: 5.3

自己引用率: 3.7%

年間論文数: 2153

NJC (New Journal of Chemistry) is a broad-based primary journal encompassing all branches of chemistry and its sub-disciplines. It contains full research articles, communications, perspectives and focus articles. This well-established journal, owned by the Centre National de la Recherche Scientifique (CNRS) of France, has been co-published with the Royal Society of Chemistry since January 1998. NJC is the forum for the publication of high-quality, original and significant work that opens new directions in chemistry or other scientific disciplines. In addition to having a significant chemical component, work published in NJC must demonstrate that it will have an impact on areas of research other than that of the reported work.

Synthesis, conformational analysis and GalNAc–lectin interactions of a constrained C-glycoside analogue of the TN antigen

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