SIGLEC-4 (MAG) Antagonists: From the Natural Carbohydrate Epitope to Glycomimetics

Schwardt, Oliver and Kelm, Soerge and Ernst, Beat. (2015) SIGLEC-4 (MAG) Antagonists: From the Natural Carbohydrate Epitope to Glycomimetics. Topics in Current Chemistry, 367. pp. 151-200.

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Official URL: http://edoc.unibas.ch/42801/

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Siglec-4, also known as myelin-associated glycoprotein (MAG), is a member of the siglec (sialic acid-binding immunoglobulin-like lectins) family. MAG binds with high preference to sialic acids α(2-3)-linked to D-galactose. Although the involvement and relevance of its sialic acid binding activity is still controversial, it could be demonstrated that interactions of MAG with sialylated gangliosides play an important role in axon stability and regeneration. In this article we describe in detail our current understanding of the biological role and the carbohydrate specificity of siglec-4. Furthermore, this review compiles the intensive research efforts leading from the identification of the minimal oligosaccharide binding epitope in gangliosides via micromolar oligosaccharide mimics to the development of small molecular weight and more drug-like sialic acid derivatives binding with low nanomolar affinities. Such compounds will be useful to elucidate MAG's biological functions, which are currently not fully understood.
Faculties and Departments:05 Faculty of Science > Departement Pharmazeutische Wissenschaften > Ehemalige Einheiten Pharmazie > Molekulare Pharmazie (Ernst)
UniBasel Contributors:Ernst, Beat and Schwardt, Oliver
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:28 Nov 2017 11:11
Deposited On:29 Nov 2016 07:01

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