Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), Departamento de Química Orgánica, Universidade de Santiago de Compostela, Santiago de Compostela, 15782, Spain.
Chemistry. 2020 Nov 17;26(64):14765-14770. doi: 10.1002/chem.202003265. Epub 2020 Oct 12.
The inherent ability of peptides to self-assemble with directional and rationally predictable interactions has fostered a plethora of synthetic two-dimensional (2D) supramolecular biomaterials. However, the design of peptides with hierarchical assembly in different dimensions across mesoscopic lengths remains a challenging task. We here describe the structural exploration of a d/l-alternating cyclic octapeptide capable of assembling one-dimensional (1D) nanotubes in water, which subsequently pack laterally to form giant 2D nanosheets up to 500 μm long with a constant 3.2 nm thickness. Specific amino acid mutations allowed the mapping of structure-assembly relationships that determine 2D self-assembly. Nine peptide modifications were studied, revealing key features in the peptide sequence that nanosheets tolerated, while a total of three peptide variants included modifications that compromised their 2D arrangement. These lessons will serve as guide and inspiration for new 2D supramolecular peptide designs.
多肽具有自组装的固有能力，能够形成具有方向性和可预测性的相互作用，从而促进了大量的二维（2D）超分子生物材料的合成。然而，设计具有层次组装的多肽，使其在不同维度上跨越介观长度仍然是一项具有挑战性的任务。在这里，我们描述了一种 d/l-交替环状八肽的结构探索，该八肽能够在水中组装一维（1D）纳米管，然后侧向堆积形成长达 500 μm 的巨大 2D 纳米片，厚度恒定为 3.2 nm。特定的氨基酸突变允许对确定 2D 自组装的结构-组装关系进行映射。研究了 9 种肽修饰，揭示了肽序列中纳米片能够容忍的关键特征，而总共有 3 种肽变体包括了破坏其 2D 排列的修饰。这些经验教训将为新的 2D 超分子肽设计提供指导和启示。
