Tailoring self-assembly of proteins on solid surfaces remains a great challenge in diverse fields, e.g., enzyme catalysis, biosensing, and biomineralization, where surface functions are retained by controlling molecular architectures. Here we use here biocombinatorially selected or bioinformatically designed solid binding short peptides which form self-assembled, long-range ordered molecular nanostructures on atomically flat surfaces. The peptides are engineered via simple sequence mutations to control fundamental processes of self-assembly, including binding to solid surfaces, surface diffusion and growth kinetics, and intermolecular interactions. Using surface imaging and chemistry, we identify specific domains of amino acids along primary sequences that steer peptide aggregation and ordering, leading to uniformly displayed residues and sequence-programmable surface chemistries. Short peptides, with easily designed sequences, offer versatile control over molecular functionalization at liquid-solid interfaces, resulting in well-defined surface properties and nanoscale topology essential in building engineered, chemically rich, bio-solid interfaces.

Programmable self-assembled peptide nanostructures on atomically flat solids

243rd National Meeting (2012)

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