[Zurück]

C. Siedler, S. Friedler, D. Ret, S. Knaus:
"Synthesis and immobilization of small molecule glycoconjugates on polymer surfaces for lectin isolation";
Poster: Danube Vltava Sava Polymer Meeting 2017, Wien; 05.09.2017 - 08.09.2017; in: "Danube Vltava Sava Polymer Meeting 2017", Book of Abstracts.com, (2017), ISBN: 978-3-9504017-6-9; S. PO-93.

Lectins are a wide spread class of proteins able to recognize and bind carbohydrates with high molecular specificity. Specific glycosylation patterns play an essential role in the pathophysiology of diseases such as autoimmune disorders, cancer and viral infections. They were suggested to be associated with altered glycan cell surface patterns resulting in a unique, disease-specific glycosylation signature. [1]
Specific glycoconjugates were immobilized as small molecule targets on suitable supports to isolate glycan-reactive lectins from dietary origin. Glycoconjugates were synthetized by coupling carbohydrates (e.g.: galactose, N-acetylglucosamine, mannose) with amino acids (serin, threonin, asparagin). The carbohydrate moiety was modified to selectively react in alpha conformation with protected amino acids. The glycoside was then covalently linked to a support matrix via a spacer. The lectin specific column material will be used for affinity chromatography and compared to commercially available less specific materials.

lectins, pathophysiology of diseases such as autoimmune disorders, cancer and viral infections, a unique, disease-specific glycosylation signature