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The binding of boronated peptides to low affinity mammalian saccharides
Author(s) -
Kowalczyk Wioleta,
Sanchez Julie,
Kraaz Phillipe,
Hutt Oliver E.,
Haylock David N.,
Duggan Peter J.
Publication year - 2018
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.23101
Subject(s) - chemistry , isothermal titration calorimetry , peptide , glycan , titration , entropy (arrow of time) , stereochemistry , enthalpy , molecule , residue (chemistry) , amino acid , biochemistry , glycoprotein , organic chemistry , thermodynamics , physics
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.