Beatriz solis cd8/9/2023 ![]() ![]() ![]() Provided correct acknowledgement is given. If you are an author contributing to an RSC publication, you do not need to request permission To request permission to reproduce material from this article, please go to the Symmetric dithiodigalactoside: strategic combination of binding studies and detection of selectivity between a plant toxin and human lectins Therefore, glycosyldisulfides have potential as chemical platform for inhibitor design. ![]() The tested glycosyldisulfide exhibits selectivity between the plant toxin and the tested human lectins, and also between these proteins. Model building indicated contact formation to be restricted to only one galactose moiety, in contrast to thiodigalactoside. In comparison, galectins were considerably less reactive, with intrafamily grading down to very minor reactivity for tandem-repeat-type galectins, as quantitated by radioassays for both domains of galectin-4. They were reflected by the structural model and the affinity on the level of toxin-exposed cells. Inhibition assays with surface-presented neoglycoprotein and in solution monitored by saturation transfer difference NMR spectroscopy, flanked by epitope mapping, as well as isothermal titration calorimetry revealed binding properties to VAA ( K a: 1560 ± 20 M −1). Based on initial evidence of this recognition ability for glycosyldisulfides by screening dynamic combinatorial libraries, we have now systematically studied dithiodigalactoside on a plant toxin ( Viscum album agglutinin) and five human lectins (adhesion/growth-regulatory galectins with medical relevance e.g. Thioglycosides offer the advantage over O-glycosides to be resistant to hydrolysis. ![]()
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