The binding of boronated peptides to low affinity mammalian saccharides

Wioleta Kowalczyk, Julie Sanchez, Phillipe Kraaz, Oliver E. Hutt, David N. Haylock, Peter J. Duggan

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2 Citations (Scopus)


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
Number of pages12
JournalPeptide Science
Issue number3
Publication statusPublished - 2018
Externally publishedYes


  • Boronolectins
  • Isothermal titration calorimetry
  • Mammalian sugars
  • Peptide boronic acids
  • Saccharide binding

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