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Updated: May 13, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Designed self-assembling peptides as templates for the synthesis of metal nanoparticles
Emmanouil Kasotakis1, Anna Mitraki
1Department of Materials Science and Technology, and Institute for Electronic Structure and Laser, Foundation for Research and Technology-Hellas, (IESL-FORTH), University of Crete, Vassilika Vouton, Heraklion, Crete, Greece.
Abstract:
Self-assembling peptides are water soluble and form biocompatible nanostructures under mild conditions through non-covalent interactions. They form supramolecular structures such as ribbons, nanotubes, and fibrils. Of particular interest is the possibility of using these peptide fibrils as templates for the growth of inorganic materials, such as metallic nanoparticles. The ability to reliably produce metal-coated fibrils with robust binding of metal nanoparticles is a vital first step towards the exploitation of these fibrils as conducting nanowires with applications in nano-circuitry. One promising strategy consists of the rational introduction of metal-binding amino acids (such as cysteine) at the level of the peptide building block. Upon assembly of the building blocks into fibrils, cysteine residues that remain accessible at the outside of the fibril core could serve as nucleation sites for metals. We will review in this chapter a case study of rationally designed cysteine-containing peptides and basic protocols for their metallization with silver, gold, and platinum nanoparticles.

