Coiled coil peptide-functionalized surfaces for reversible molecular binding

We studied the conformational and self-assembly properties of de novo peptides derived from the structure of the yeast transcriptional activator GCN4 in solution and on surfaces. We showed how the pH and the polarity of the solvent directed peptide conformation and assembly. The peptides self-assembled into a coiled coil structure below pH 5 whereas they disassembled above pH 7. The presence of acetonitrile in the peptide solution influenced the peptide's ability to assemble into a coiled coil structure while retaining its alpha-helix conformation. We used these properties to control the peptide packing density on gold surfaces and demonstrated that such peptide-engineered surfaces could be used for reversible molecular binding by utilising functionalised gold nanoparticles.