title: Stacking interactions by two Phe side chains stabilize and orient assemblies of even the minimal amphiphilic β-sheet motif.
abstract: Here we demonstrate that the smallest possible motif of the amphiphilic and pleated β-strand structure can be generated using tri-peptides stabilized by π-π stacking interactions. Monitoring the early stages of Phe-Glu-Phe fibril formation revealed unique angular orientations. Phe-Glu-Phe fibrils were further exploited as adsorbing templates for metal ions.
authors.forename: Shlomo
authors.initials: S
authors.lastname: Zarzhitsky
authors.affiliation: Avram and Stella Goldstein-Goren Department of Biotechnology Engineering, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel. hannarap@bgu.ac.il.
authors.forename: Zarzhitsky
authors.initials: Z
authors.lastname: Shlomo
authors.forename: T P
authors.initials: TP
authors.lastname: Vinod
authors.forename: Raz
authors.initials: R
authors.lastname: Jelinek
authors.forename: Hanna
authors.initials: H
authors.lastname: Rapaport
mesh_terms: D005973:Glutamine / Q000737:chemistry*; D006046:Gold / Q000737:chemistry; D043942:Nanotubes / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012834:Silver / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D005973:Glutamine; D012834:Silver; D010649:Phenylalanine; D006046:Gold