Combining glycocluster synthesis with protein engineering: an approach to probe into the significance of linker length in a tandem-repeat-type lectin (galectin-4).

摘要: Complementarity in lectin-glycan interactions situ is assumed to involve spatial features both the lectin and glycan, giving a functional meaning structural aspects of beyond its carbohydrate-binding site. In combining protein engineering with glycocluster synthesis, it shown that natural linker length tandem-repeat-type human (galectin-4) determines binding properties two assays (using surface-presented glycoprotein cell surface assays). The types tested included bivalent lactosides based on tertiary amides terephthalic, isophthalic, 2,6-naphthalic oxalic acids as well H(type 2) trisaccharides grafted secondary/tertiary terephthalamides triazole-linker-containing cores. presented data reveal marked change susceptibility test compounds when turning proto-type-like display. testing glycoclusters suggested general strategy help delineate significance distinct lectins their contact sites glycan.