title: Coassembly of enantiomeric amphipathic peptides into amyloid-inspired rippled β-sheet fibrils.
abstract: Amphipathic peptides composed of alternating hydrophobic and hydrophilic amino acids self-assemble into amyloid-inspired, β-sheet nanoribbon fibrils. Herein, we report a new fibril type that is formed from equimolar mixtures of enantiomeric amphipathic peptides (L- and D-(FKFE)(2)). Spectroscopic analysis indicates that these peptides do not self-sort and assemble into enantiomeric fibrils composed of all-l and all-d peptides, but rather coassemble into fibrils that contain alternating L- and D-peptides in a "rippled β-sheet" orientation. Isothermal titration calorimetry indicates an enthalpic advantage for rippled β-sheet coassembly compared to self-sorted β-sheet assembly of enantiomeric peptides.
authors.affiliation: Department of Chemistry, University of Rochester, Rochester, New York 14627-0216, United States.
authors.forename: Ria J
authors.initials: RJ
authors.lastname: Swanekamp
authors.forename: John T M
authors.initials: JT
authors.lastname: DiMaio
authors.forename: Charles J
authors.initials: CJ
authors.lastname: Bowerman
authors.forename: Bradley L
authors.initials: BL
authors.lastname: Nilsson
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared
chemical_list: D000596:Amino Acids; D000682:Amyloid; D010455:Peptides