ABSTRACT The head-to-tail cyclic hexapeptide, [cyclo(Val-Thr)3], was found to bind to a range of anions in DMSO-d6 with higher affinity for tetrahedral oxo-anions than halides. 1H NMR spectroscopy indicated that anion binding results in an overall change in peptide conformation with the binding of both sulphate and selenate leading to similar peptide conformations. In the more competitive solvent mixture of 2:8 v/v H2O/DMSO-d 6 this cyclic peptide displayed five-fold stronger binding to sulphate than to selenate. Graphical abstract

中文翻译：

---

使用简单环肽进行阴离子识别

摘要 发现头对尾环状六肽 [cyclo(Val-Thr)3] 与 DMSO-d6 中的一系列阴离子结合，对四面体氧阴离子的亲和力高于卤化物。1 H NMR 光谱表明阴离子结合导致肽构象的整体变化，硫酸盐和硒酸盐的结合导致相似的肽构象。在更具竞争力的 2:8 v/v H2O/DMSO-d 6 溶剂混合物中，这种环肽与硫酸盐的结合比与硒酸盐的结合强五倍。图形概要