Abstract:
:In Alzheimer's disease, beta-amyloid peptides (betaA(1-40) and betaA(1-42)) are deposited on the brain cell surfaces as neurotoxic plaques. Some reports indicate that small heat shock proteins, Hsp27 and alphaB-crystallin, colocalize in the plaques, but their functions are not known. Interaction between betaA and alphaB-crystallin must be determined in order to understand the role of alphaB-crystallin in betaA fibril formation. We used a pyrene (Pyr)-labeled betaA(1-40) in a fluorescence energy transfer experiment. Upon incubation together at 37 degrees C, energy transfer between Trp of alphaB-crystallin and Pyr of Pyr-labeled betaA was observed, indicating that betaA participated in subunit exchange of alphaB-crystallin, which promoted fibril formation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Liang JJdoi
10.1016/s0014-5793(00)02136-0keywords:
subject
Has Abstractpub_date
2000-11-03 00:00:00pages
98-101issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02136-0journal_volume
484pub_type
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