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Molecular recognition of ConA and mannose on liposome surface

Multivalent glycolipid derivatives are a new class of compounds which may be of interest for glycosylation of liposome surfaces and targeted drug delivery1, 2. For a selective transport to the target immunocompetent cells, these compounds comprise mannose molecules in their structure which bind specifically to C- Type Lectin Receptors. The design and synthesis of multivalent glycocluster requires the conjugation of biologically relevant carbohydrate epitopes functionalized with linker arms to multivalent core scaffolds. In order to study the influence of multivalency of the carbohydrate part of glycolipid molecule to the affinity and recognition of the targeted receptors, the mono-, di- and tetra-mannosyl lipoconjugates were synthesized. The synthesized compounds were easily incorporated into liposomes and the mannosylated liposome were characterized by DLS and AFM. Spectrofotometric3 and carbohydrate liposomal quartz crystal microbalance based assays 4 have been established for studying carbohydrate– lectin binding. It was demonstrated that liposomes with incorporated mannosyl- lypoconjugates were effectively recognized by the Con A. It was shown that lectine affinity increases with the increase of the number of molecules of mannose in glycolipid conjugates. Also, it was demonstrated that the mannosylated liposomes can be a useful model for investigation of specific interactions with lectin receptors.

Surface molecular recognition; ConA; Mannose receptors; Liposomes

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