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Interaction between β‐amyloid and lens αB‐crystallin
Author(s) -
Liang Jack J.-N
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02136-0
Subject(s) - crystallin , pyrene , chemistry , biophysics , colocalization , heat shock protein , fibril , protein subunit , biochemistry , microbiology and biotechnology , biology , organic chemistry , gene
In Alzheimer's disease, β‐amyloid peptides (βA 1–40 and βA 1–42 ) are deposited on the brain cell surfaces as neurotoxic plaques. Some reports indicate that small heat shock proteins, Hsp27 and αB‐crystallin, colocalize in the plaques, but their functions are not known. Interaction between βA and αB‐crystallin must be determined in order to understand the role of αB‐crystallin in βA fibril formation. We used a pyrene (Pyr)‐labeled βA 1–40 in a fluorescence energy transfer experiment. Upon incubation together at 37°C, energy transfer between Trp of αB‐crystallin and Pyr of Pyr‐labeled βA was observed, indicating that βA participated in subunit exchange of αB‐crystallin, which promoted fibril formation.