Materials World Network: Fundamentals of Peptide Materials - Experimental and Simulation Probes

肽已成为一类重要的生物相容性，环境友好，可持续的材料替代品。一方面，它们可以被设计成自组装成广泛的纳米结构，作为组织支架、生物传感器、药物递送剂和无机材料的牺牲模板。另一方面，它们提供了独特的方法来修改具有表面保护，疏水，抗生素或粘合能力的固体界面。然而，它们的理性工程由于缺乏对它们的许多不同分子相互作用（例如氢键、静电和疏水力）协同或竞争产生复杂、合作、多体集体行为的方式的详细理解而受到限制。本研究将最先进的原子力显微镜（AFM）与先进的分子模拟研究相结合，以获得肽-肽相互作用的创新基础见解，特别是它们在固/液界面介导相互作用的能力。使用一个独特的灵活的模型肽重复支架，精确可控的序列和相互作用肽的数量将被检查，从而相互作用和合作可以调整与严格的控制。详细的AFM测量将与由平衡、定量全原子模拟开发的分子图像进行比较，这些模拟探测了真正潜在的、平衡的相互作用景观。特别是疏水和电荷相互作用之间的平衡以及多肽相互作用的协同效应，将以系统和分层的方式进行研究。

Peptides have emerged as an important class of biocompatible, environmentally friendly, sustainable material alternatives. On the one hand, they can be engineered to self-assemble into a broad array of nanostructures important as tissue scaffolds, biosensors, drug delivery agents, and sacrificial templates for inorganic materials. On the other, they offer unique ways to modify solid interfaces with surface protecting, hydrophobic, antibiotic, or adhesive capabilities. However, their rational engineering is limited by lack of a detailed understanding of the ways in which their many distinct molecular interactions - hydrogen bonding, electrostatic, and hydrophobic forces, for example - act in concert or competition to produce complex, cooperative, many-body collective behavior. This study combines state-of-the-art atomic force microscopy (AFM) hand-in-hand with advanced molecular simulation studies to obtain innovative fundamental insights into peptide-peptide interactions and, in particular, their ability to mediate interactions at solid/liquid interfaces. Using a uniquely flexible model peptide repeat scaffold, precisely controllable sequences and numbers of interacting peptides will be examined, whereby interactions and cooperativities can be tuned with exacting control. Detailed AFM measurements will be compared to molecular pictures developed by equilibrium, quantitative all-atom simulations that probe true underlying, equilibrium interaction landscapes. In particular, the balance between hydrophobic and charge interactions and the effect of cooperative, multi-peptide interactions will be studied in a systematic and hierarchical manner.