Gold Decorated Peptide Amphiphile Templates for Directed Silver Nanorods Growth

Peptides are versatile building blocks that can be designed to assume particular structure with respect to predetermined function and biological activity. Tailoring the exact sequence of amino acids in peptides allows fine tuning of mechanical and chemical properties, along with self-assembly kinetic. Amphiphilic and anionic β-sheet peptides may form hydrogels at near physiological pH values. Our group has previously studied peptides with the amphiphilic motif (Phe-X) in peptides such as Pro-Glu-(Phe-Glu)5 -Pro. In the current study we were intrigued to explore whether an amphiphilic tripeptide, exhibiting one β-pleated motif, i.e. Phe-X-Phe with X = hydrophilic amino acid can be triggered to self-assemble into b-sheet fibrils. Relying on the crucial role of aromatic stacking interactions as the driving force in molecular self-assembly, we explored the self-assembly of this family of peptides with X = Glu\Lys\Cys\Thr. All these peptides were found to constitute self-supporting hydrogels under various conditions.