Controlling Self-Assembly of Engineered Peptides on Graphite by Rational Mutation

Citations Over TimeTop 10% of 2012 papers

Abstract

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.

Related Papers

• → Rational Design of p53, an Intrinsically Unstructured Protein, for the Fabrication of Novel Molecular Sensors(2005)12 cited
• → Tunable morphologies from solution self-assembly of diblock copolymers under nanoscale confinement(2019)4 cited
• → Introduction to Directed Evolution and Rational Design as Protein Engineering Techniques(2023)3 cited
• → Formation of Nanostructures by Self‐Assembly(2010)1 cited
• → Protein Engineering: Methods and Applications(2017)1 cited