title: Combination of theoretical and experimental approaches for the design and study of fibril-forming peptides.
abstract: Self-assembling peptides that can form supramolecular structures such as fibrils, ribbons, and nanotubes are of particular interest to modern bionanotechnology and materials science. Their ability to form biocompatible nanostructures under mild conditions through non-covalent interactions offers a big biofabrication advantage. Structural motifs extracted from natural proteins are an important source of inspiration for the rational design of such peptides. Examples include designer self-assembling peptides that correspond to natural coiled-coil motifs, amyloid-forming proteins, and natural fibrous proteins. In this chapter, we focus on the exploitation of structural information from beta-structured natural fibers. We review a case study of short peptides that correspond to sequences from the adenovirus fiber shaft. We describe both theoretical methods for the study of their self-assembly potential and basic experimental protocols for the assessment of fibril-forming assembly.
authors.affiliation: Department of Physics, University of Cyprus, 20537, CY1678, Nicosia, Cyprus.
authors.forename: Phanourios
authors.initials: P
authors.lastname: Tamamis
authors.forename: Emmanouil
authors.initials: E
authors.lastname: Kasotakis
authors.forename: Georgios
authors.initials: G
authors.lastname: Archontis
authors.forename: Anna
authors.initials: A
authors.lastname: Mitraki
mesh_terms: D000682:Amyloid / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry; D010452:Peptide Biosynthesis / Q000502:physiology*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D000682:Amyloid; D010455:Peptides