title: Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils.
abstract: The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.
authors.affiliation: Department of Chemistry, Ben-Gurion University of the Negev, Beér-Sheva 84105, Israel.
authors.forename: Yoav
authors.initials: Y
authors.lastname: Raz
authors.forename: Boris
authors.initials: B
authors.lastname: Rubinov
authors.forename: Maayan
authors.initials: M
authors.lastname: Matmor
authors.forename: Hanna
authors.initials: H
authors.lastname: Rapaport
authors.forename: Gonen
authors.initials: G
authors.lastname: Ashkenasy
authors.forename: Yifat
authors.initials: Y
authors.lastname: Miller
mesh_terms: D056004:Molecular Dynamics Simulation; D009154:Mutation; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides