Self-Assembling Amyloid Sequences as Scaffolds for Material Design: A Case Study of Building Blocks Inspired From the Adenovirus Fiber Protein

In the last two decades the study of the properties of biological self-organization has created a separate area of research, ranging from biomedicine and biotechnology to materials science and nanotechnology. In particular, the design of self-assembling protein and peptide building blocks is often achieved by drawing inspiration from natural fibrous proteins such as collagen, elastin, silk, and spider silks that are built up from repetitive sequences. Self-assembling proteins and peptides are water soluble and biocompatible nanostructures formed spontaneously under mild conditions through non-covalent interactions. They form supramolecular structures such as ribbons, nanotubes, and fibers. The wide range of chemical functionalities found in peptides (i.e., 20 amino acids) enables the design and engineering of specific interactions with target materials for potential technological applications. Moreover, with the aid of computational methods, tailor made modifications can be inserted for the << on-demand >> design of functional amyloid materials binding to ions or compounds. Technologically, the self-organized structures can be used as templates for the growth of inorganic materials, such as metallic nanoparticles (silver, gold, and platinum), silica, calcium phosphates etc. Self-assembling peptides may also create hydrogels and entangled fibrous networks that can be used as scaffolds for attachment, growth and proliferation of living cells, allowing tissue repair and engineering. In this short review we summarize the progress made in the field with emphasis on our progress on how to translate fundamental structural knowledge from the adenovirus fiber protein into self-assembling nanomaterials targeted for novel applications.