WestCHEM, Department of Pure and Applied Chemistry, University of Strathclyde , Glasgow, U.K.
Biomacromolecules. 2013 Dec 9;14(12):4368-76. doi: 10.1021/bm401319c. Epub 2013 Nov 27.
Molecular self-assembly provides a versatile route for the production of nanoscale materials for medical and technological applications. Herein, we demonstrate that the cooperative self-assembly of amphiphilic small molecules and proteins can have drastic effects on supramolecular nanostructuring of resulting materials. We report that mesoscale, fractal-like clusters of proteins form at concentrations that are orders of magnitude lower compared to those usually associated with molecular crowding at room temperature. These protein clusters have pronounced effects on the molecular self-assembly of aromatic peptide amphiphiles (fluorenylmethoxycarbonyl- dipeptides), resulting in a reversal of chiral organization and enhanced order through templating and binding. Moreover, the morphological and mechanical properties of the resultant nanostructured gels can be controlled by the cooperative self-assembly of peptides and protein fractal clusters, having implications for biomedical applications where proteins and peptides are both present. In addition, fundamental insights into cooperative interplay of molecular interactions and confinement by clusters of chiral macromolecules is relevant to gaining understanding of the molecular mechanisms of relevance to the origin of life and development of synthetic mimics of living systems.
分子自组装为医学和技术应用提供了一种生产纳米材料的通用途径。在此，我们证明了两亲性小分子和蛋白质的协同自组装对所得材料的超分子纳米结构具有巨大影响。我们报告说，在与室温下分子拥挤通常相关的浓度下，蛋白质形成介观、分形样的簇。这些蛋白质簇对芳香族肽两亲物（芴甲氧羰基-二肽）的分子自组装有明显影响，通过模板和结合导致手性组织的反转和增强有序性。此外，通过肽和蛋白质分形簇的协同自组装可以控制所得纳米结构凝胶的形态和机械性能，这对蛋白质和肽都存在的生物医学应用具有重要意义。此外，深入了解手性大分子簇对分子相互作用和限制的协同相互作用，对于理解与生命起源和合成生命系统模拟物的发展相关的分子机制具有重要意义。
