Genetically Engineered Materials Science and Engineering Center, Department of Materials Science and Engineering, University of Washington, Seattle, Washington 98195, United States.
ACS Nano. 2012 Feb 28;6(2):1648-56. doi: 10.1021/nn204631x. Epub 2012 Jan 18.
Self-assembly of proteins on surfaces is utilized in many fields to integrate intricate biological structures and diverse functions with engineered materials. Controlling proteins at bio-solid interfaces relies on establishing key correlations between their primary sequences and resulting spatial organizations on substrates. Protein self-assembly, however, remains an engineering challenge. As a novel approach, we demonstrate here that short dodecapeptides selected by phage display are capable of self-assembly on graphite and form long-range-ordered biomolecular nanostructures. Using atomic force microscopy and contact angle studies, we identify three amino acid domains along the primary sequence that steer peptide ordering and lead to nanostructures with uniformly displayed residues. The peptides are further engineered via simple mutations to control fundamental interfacial processes, including initial binding, surface aggregation and growth kinetics, and intermolecular interactions. Tailoring short peptides via their primary sequence offers versatile control over molecular self-assembly, resulting in well-defined surface properties essential in building engineered, chemically rich, bio-solid interfaces.
蛋白质在表面上的自组装在许多领域被用于将复杂的生物结构和多样化的功能与工程材料集成在一起。在生物固-液界面控制蛋白质依赖于建立它们的一级序列和在基底上的空间组织之间的关键相关性。然而，蛋白质自组装仍然是一个工程挑战。作为一种新方法，我们在这里展示了通过噬菌体展示选择的短十二肽能够在石墨上自组装并形成长程有序的生物分子纳米结构。使用原子力显微镜和接触角研究，我们确定了一级序列中沿三个氨基酸结构域引导肽的有序排列，并导致具有均匀展示残基的纳米结构。通过简单的突变进一步对这些肽进行工程设计以控制基本的界面过程，包括初始结合、表面聚集和生长动力学以及分子间相互作用。通过其一级序列对短肽进行定制化处理为分子自组装提供了多种控制手段，从而产生了在构建工程化、化学丰富的生物固-液界面中至关重要的明确定义的表面性质。
