title: Self-assembly and self-replication of short amphiphilic β-sheet peptides.
abstract: Most self-replicating peptide systems are made of α-helix forming sequences. However, it has been postulated that shorter and simpler peptides may also serve as templates for replication when arranged into well-defined structures. We describe here the design and characterization of new peptides that form soluble β-sheet aggregates that serve to significantly accelerate their ligation and self-replication. We then discuss the relevance of these phenomena to early molecular evolution, in light of additional functionality associated with β-sheet assemblies.
authors.affiliation: Department of Chemistry, Ben Gurion University of Negev, Beer Sheva, Israel.
authors.forename: Valery
authors.initials: V
authors.lastname: Bourbo
authors.forename: Maayan
authors.initials: M
authors.lastname: Matmor
authors.forename: Elina
authors.initials: E
authors.lastname: Shtelman
authors.forename: Boris
authors.initials: B
authors.lastname: Rubinov
authors.forename: Nurit
authors.initials: N
authors.lastname: Ashkenasy
authors.forename: Gonen
authors.initials: G
authors.lastname: Ashkenasy
mesh_terms: D019418:Evolution, Chemical; D000069497:Origin of Life; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017433:Protein Structure, Secondary; D013501:Surface-Active Agents / Q000737:chemistry*
chemical_list: D010455:Peptides; D013501:Surface-Active Agents