Interaction between β‐amyloid and lens αB‐crystallin

FEBS Letters

Liang, Jack J.-N¹ 

[1] Center for Ophthalmic Research, Brigham and Women's Hospital, Department of Ophthalmology, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA

关键词: β-Amyloid;    αB-Crystallin;    Fluorescence;    Fluorescence energy transfer;    Circular dichroism;   

DOI  :  10.1016/S0014-5793(00)02136-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown