Center for Multiscale Chiral Architectures, Department of Chemistry, Korea Advanced Institute of Science and Technology, Yuseong-gu, Daejeon, 34141, Korea.
Korea Research Institute of Chemical Technology, Yuseong-gu, Daejeon, 34114, Korea.
Small. 2021 Sep;17(36):e2102525. doi: 10.1002/smll.202102525. Epub 2021 Jul 26.
The synthesis of morphologically well-defined peptidic materials via self-assembly is challenging but demanding for biocompatible functional materials. Moreover, switching morphology from a given shape to other predictable forms by molecular modification of the identical building block is an even more complicated subject because the self-assembly of flexible peptides is prone to diverge upon subtle structural change. To accomplish controllable morphology transformation, systematic self-assembly studies are performed using congener short β-peptide foldamers to find a minimal structural change that alters the self-assembled morphology. Introduction of oxygen-containing β-amino acid (ATFC) for subtle electronic perturbation on hydrophobic foldamer induces a previously inaccessible solid-state conformational split to generate the most susceptible modification site for morphology transformation of the foldamer assemblies. The site-dependent morphological switching power of ATFC is further demonstrated by dual substitution experiments and proven by crystallographic analyses. Stepwise morphology transformation is shown by modifying an identical foldamer scaffold. This study will guide in designing peptidic molecules from scratch to create complex and biofunctional assemblies with nonspherical shapes.
通过自组装合成形态良好定义的肽材料具有挑战性，但对于生物相容的功能材料来说却是必需的。此外，通过相同构建块的分子修饰将形态从给定形状切换为其他可预测的形状更是一个复杂的课题，因为柔性肽的自组装很容易在细微的结构变化下发生偏离。为了实现可控的形态转变，使用同源短 β-肽折叠体进行了系统的自组装研究，以找到改变自组装形态的最小结构变化。在疏水性折叠体上引入含氧的β-氨基酸（ATFC）可对电子进行细微的扰动，从而在以前无法进入的固态构象中产生分裂，从而为折叠体组装的形态转变生成最易受影响的修饰部位。通过双取代实验进一步证明了 ATFC 的部位依赖性形态切换能力，并通过晶体学分析得到证实。通过修饰相同的折叠体支架展示了逐步的形态转变。这项研究将有助于从头设计肽分子，以创建具有非球形形状的复杂和生物功能的组装体。
