Light-Controlled Toxicity of Engineered Amyloid β-Peptides

• Published in: Chembiochem : a European journal of chemical biology Vol. 13; no. 18; pp. 2657 - 2660
• Main Authors: Hoppmann, Christian, Barucker, Christian, Lorenz, Dorothea, Multhaup, Gerd, Beyermann, Michael
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 21.12.2012; WILEY‐VCH Verlag
• Subjects: Alzheimer's disease; Amino Acid Sequence; amyloid beta-peptides; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - toxicity; azobenzene; Cell Line, Tumor; Humans; isomerization; Light; light-directed disassembly; Molecular Sequence Data; Peptide Fragments - chemistry; Peptide Fragments - toxicity; Protein Engineering; Protein Multimerization - radiation effects; Protein Structure, Secondary - radiation effects
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201200605

Aggregation of amyloid β (Aβ1–42), causing toxicity, is a critical step in Alzheimer's disease (AD). AD studies are difficult to compare because Aβ1–42 aggregation is poorly controllable under physiological conditions. To control aggregation and toxicity, we engineered light‐switchable Aβ1–42 analogues that enable controllable conversion of nontoxic fibrils into toxic oligomers simply by illumination.