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.

中文翻译：

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硼化肽与低亲和力哺乳动物糖的结合。


测试了一个由 54 个成员组成的硼化八肽文库，其中除硼化残基外的所有残基都是蛋白原性的，测试了其与哺乳动物聚糖末端常见的一组糖的亲和力。在进行高通量染料置换测定实验后，人们的注意力集中在等温滴定量热法作为提供可靠亲和力数据（包括结合焓和熵）的工具上。少数硼化肽对 N-乙酰神经氨酸表现出比甲基-α-d-吡喃半乳糖苷、甲基-α/β-l-吡喃岩藻糖苷和 N-乙酰基-d-葡萄糖胺更高的亲和力和显着的选择性。热力学数据表明，对于大多数研究的硼化肽，糖结合与熵的显着增加相关，这可能是由于糖和/或肽周围的半有序水分子的置换所致。