title: Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ(1-23) using an unnatural amino acid.
abstract: We identify distinct site-specific dynamics over the time course of Aβ1-23 amyloid formation by using an unnatural amino acid, p-cyanophenylalanine, as a sensitive fluorescent and Raman probe. Our results also suggest the key role of an edge-to-face aromatic interaction in the conformational conversion to form and stabilize β-sheet structure.
authors: Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL 33431, USA. ddu@fau.edu.
authors: Haiyang
authors: H
authors: Liu
authors: Richard
authors: R
authors: Lantz
authors: Patrick
authors: P
authors: Cosme
authors: Nelson
authors: N
authors: Rivera
authors: Carlos
authors: C
authors: Andino
authors: Walter G
authors: WG
authors: Gonzalez
authors: Andrew C
authors: AC
authors: Terentis
authors: Ewa P
authors: EP
authors: Wojcikiewicz
authors: Rolando
authors: R
authors: Oyola
authors: Jaroslava
authors: J
authors: Miksovska
authors: Deguo
authors: D
authors: Du
mesh_terms: D000409:Alanine / Q000031:analogs & derivatives* / Q000737:chemistry; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009570:Nitriles / Q000737:chemistry*; D017433:Protein Structure, Secondary; D010649:Phenylalanine / Q000031:analogs & derivatives
chemical_list: D000409:Alanine; D016229:Amyloid beta-Peptides; D009570:Nitriles; C530634:p-cyanophenylalanine; D010649:Phenylalanine