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Light‐Controlled Toxicity of Engineered Amyloid β‐Peptides
Author(s) -
Hoppmann Christian,
Barucker Christian,
Lorenz Dorothea,
Multhaup Gerd,
Beyermann Michael
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200605
Subject(s) - toxicity , amyloid (mycology) , chemistry , peptide , computational biology , biochemistry , pharmacology , nanotechnology , medicine , biology , materials science , organic chemistry , inorganic chemistry
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.