The binding of boronated peptides to low affinity mammalian saccharides. Issue 3 (28th May 2018)

• Record Type: Journal Article
• Authors: Kowalczyk, Wioleta; Sanchez, Julie; Kraaz, Phillipe; Hutt, Oliver E.; Haylock, David N.; Duggan, Peter J.
• Other Names: Craik David J. guestEditor.; Payne Richard J. guestEditor.
• Is Part Of: Peptide science. Volume 110:Issue 3(2018)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2018-05-28
• Subjects: boronolectins -- isothermal titration calorimetry -- mammalian sugars -- peptide boronic acids -- saccharide binding; Peptides -- Periodicals; 572.6505
• DOI: 10.1002/pep2.23101
• Languages: English
• ISSNs: 2475-8817

Abstract

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. Abstract :