Department of Chemical and Pharmaceutical Sciences, University of Trieste, Trieste, Italy.
Elettra Sincrotrone Trieste, Trieste, Italy.
J Pept Sci. 2024 May;30(5):e3559. doi: 10.1002/psc.3559. Epub 2023 Dec 18.
This work describes the self-assembly behavior of heterochiral, aliphatic dipeptides, l-Leu-d-Xaa (Xaa = Ala, Val, Ile, Leu), in green solvents such as acetonitrile (MeCN) and buffered water at neutral pH. Interestingly, water plays a structuring role because at 1% v/v, it enables dipeptide self-assembly in MeCN to yield organogels, which then undergo transition towards crystals. Other organic solvents and oils were tested for gelation, and metastable gels were formed in tetrahydrofuran, although at high peptide concentration (80 mM). Single-crystal X-ray diffraction revealed the dipeptides' supramolecular packing modes in amphipathic layers, as opposed to water channels reported for the homochiral Leu-Leu, or hydrophobic columns reported for homochiral Leu-Val and Leu-Ile.
这项工作描述了手性脂肪族二肽 l-Leu-d-Xaa（Xaa = Ala、Val、Ile、Leu）在绿色溶剂（如乙腈和缓冲水）中的自组装行为，在中性 pH 下。有趣的是，水起到了结构作用，因为在 1%v/v 的浓度下，它能够使二肽在乙腈中自组装形成有机凝胶，然后向晶体转变。还测试了其他有机溶剂和油类的凝胶化性能，在四氢呋喃中形成了亚稳态凝胶，但需要高浓度的肽（80mM）。单晶 X 射线衍射揭示了二肽在两亲层中的超分子堆积模式，与报道的手性 Leu-Leu 的水通道或报道的手性 Leu-Val 和 Leu-Ile 的疏水性柱不同。
