The binding of boronated peptides to low affinity mammalian saccharides Academic Article uri icon

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.

authors

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

publication date

  • 2018