title: Light-controlled toxicity of engineered amyloid β-peptides.
abstract: Aggregation of amyloid β (Aβ(1-42)), causing toxicity, is a critical step in Alzheimer's disease (AD). AD studies are difficult to compare because Aβ(1-42) aggregation is poorly controllable under physiological conditions. To control aggregation and toxicity, we engineered light-switchable Aβ(1-42) analogues that enable controllable conversion of nontoxic fibrils into toxic oligomers simply by illumination.
authors.affiliation: Department of Chemical Biology, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany. choppmann@salk.edu
authors.forename: Christian
authors.initials: C
authors.lastname: Hoppmann
authors.forename: Christian
authors.initials: C
authors.lastname: Barucker
authors.forename: Dorothea
authors.initials: D
authors.lastname: Lorenz
authors.forename: Gerd
authors.initials: G
authors.lastname: Multhaup
authors.forename: Michael
authors.initials: M
authors.lastname: Beyermann
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000633:toxicity*; D045744:Cell Line, Tumor; D006801:Humans; D008027:Light; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000633:toxicity*; D015202:Protein Engineering; D055503:Protein Multimerization / Q000528:radiation effects*; D017433:Protein Structure, Secondary / Q000528:radiation effects
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)