Biomimetic Tweezers for N-Glycans: Selective Recognition of the Core GlcNAc(2) Disaccharide of the Sialylglycopeptide SGP
In recent years, glycomics have shown how pervasive the role of carbohydrates in biological systems is and how chemical tools are essential to investigate glycan function and modulate carbohydrate-mediated processes. Biomimetic receptors for carbohydrates can carry out this task but, although signif...
| Autores: | , , , , , , |
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| Tipo de documento: | artigo |
| Data de publicação: | 2023 |
| País: | España |
| Recursos: | Universidad del País Vasco |
| Repositório: | Addi. Archivo Digital para la Docencia y la Investigación |
| OAI Identifier: | oai:addi.ehu.eus:10810/61055 |
| Acesso em linha: | http://hdl.handle.net/10810/61055 |
| Access Level: | Acceso aberto |
| Palavra-chave: | biomimetic artificial receptors carbohydrates chitobiose glycan molecular recognition |
| Resumo: | In recent years, glycomics have shown how pervasive the role of carbohydrates in biological systems is and how chemical tools are essential to investigate glycan function and modulate carbohydrate-mediated processes. Biomimetic receptors for carbohydrates can carry out this task but, although significant affinities and selectivities toward simple saccharides have been achieved, targeting complex glycoconjugates remains a goal yet unattained. In this work we report the unprecedented recognition of a complex biantennary sialylglycopeptide (SGP) by a tweezers-shaped biomimetic receptor, which selectively binds to the core GlcNAc2 disaccharide of the N-glycan with an affinity of 170 μM. Because of the simple structure and the remarkable binding ability, this biomimetic receptor can represent a versatile tool for glycoscience, opening the way to useful applications. |
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