Cooperative self-assembly of peptide gelators and proteins.
Cooperative self-assembly of peptide gelators and proteins.
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DOI：
10.1021/bm401319c
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发表时间：
2013-12-09
影响因子：
6.2
通讯作者：
Ulijn, Rein V.
中科院分区：
文献类型：
--
作者：
Javid, Nadeem;Roy, Sangita;Zelzer, Mischa;Yang, Zhimou;Sefcik, Jan;Ulijn, Rein V.
分子自组装为生产用于医疗和技术应用的纳米材料提供了一条通用的途径。在此，我们证明了两亲性小分子和蛋白质的合作自组装可以对所得材料的超分子纳米结构产生巨大影响。我们报告说，在中尺度，分形的蛋白质簇形成的浓度比通常与室温下的分子拥挤有关的浓度低几个数量级。这些蛋白质团簇对芳香肽两亲分子（氟烯基甲氧羰基-二肽）的分子自组装有明显的影响，通过模板和结合导致手性组织的逆转和秩序的增强。此外，由此产生的纳米结构凝胶的形态和力学性能可以通过多肽和蛋白质分形簇的合作自组装来控制，这对同时存在蛋白质和多肽的生物医学应用具有重要意义。此外，对分子相互作用和手性大分子簇限制的合作相互作用的基本见解，有助于理解与生命起源和生命系统合成模拟物发展相关的分子机制。
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.
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