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Publication Abstract from PubMed

The small 3-O-sulfated galactose head group of sulfatides, an abundant glycosphingolipid class, poses the (sphinx-like) riddle on involvement of glycan bridging by tissue lectins (sugar code). First, synthesis of head group derivatives for functionalization of amphiphilic dendrimers is performed. Aggregation of resulting (biomimetic) vesicles, alone or in combination with lactose, demonstrates bridging by a tissue lectin (galectin-4). Physiologically, this can stabilize glycolipid-rich microdomains (rafts) and associate sulfatide-rich regions with specific glycoproteins. Further testing documents importance of heterobivalency and linker length. Structurally, sulfatide recognition by galectin-8 is shown to involve sphingosine's OH group as substitute for the 3'-hydroxyl of glucose of lactose. These discoveries underscore functionality of this small determinant on biomembranes intracellularly and on the cell surface. Moreover, they provide a role model to examine counterreceptor capacity of more complex glycans of glycosphingolipids and to start their bottom-up glycotope surface programming.

Probing sulfatide-tissue lectin recognition with functionalized glycodendrimersomes.,Murphy PV, Romero A, Xiao Q, Ludwig AK, Jogula S, Shilova NV, Singh T, Gabba A, Javed B, Zhang D, Medrano FJ, Kaltner H, Kopitz J, Bovin NV, Wu AM, Klein ML, Percec V, Gabius HJ iScience. 2020 Dec 10;24(1):101919. doi: 10.1016/j.isci.2020.101919. eCollection , 2021 Jan 22. PMID:33409472^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.