The binding of boronated peptides to low affinity mammalian saccharides

Wioleta Kowalczyk, Julie Sanchez, Phillipe Kraaz, Oliver Hutt, David Haylock, Peter Duggan

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    Abstract

    A 54-member library of boronated octapeptides, with all but the boronated residue being proteinogenic, was tested for affinity to a set of saccharides commonly found on the terminus of mammalian glycans. After experimentation with a high-throughput dye-displacement assay, attention was focused on isothermal titration calorimetry as a tool to provide reliable affinity data, including enthalpy and entropy of binding. A small number of boronated peptides showed higher affinity and significant selectivity for N-acetylneuraminic acid over methyl-α-d-galactopyranoside, methyl-α/β-l-fucopyranoside and N-acetyl-d-glucosamine. Thermodynamic data showed that for most of the boronated peptides studied, saccharide binding was associated with a significant increase in entropy, presumably resulting from the displacement of semiordered water molecules from around the sugar and/or peptide.

    Original languageEnglish
    Article numbere23101
    JournalPeptide Science
    Volume110
    Issue number3
    DOIs
    Publication statusPublished - 2018

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    Kowalczyk, W., Sanchez, J., Kraaz, P., Hutt, O., Haylock, D., & Duggan, P. (2018). The binding of boronated peptides to low affinity mammalian saccharides. Peptide Science, 110(3), [e23101]. https://doi.org/10.1002/pep2.23101