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Kinesin‐1 inhibits the aggregation of amyloid‐β peptide as detected by fluorescence cross‐correlation spectroscopy
Author(s) -
Zheng Yanpeng,
Tian Shijun,
Peng Xianglei,
Yang Jingfa,
Fu Yuanhui,
Jiao Yueying,
Zhao Jiang,
He Jinsheng,
Hong Tao
Publication year - 2016
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 - 10.1002/1873-3468.12137
Subject(s) - kinesin , chemistry , fluorescence correlation spectroscopy , green fluorescent protein , biophysics , amyloid (mycology) , fluorescence , fluorescence spectroscopy , microbiology and biotechnology , amyloid precursor protein , protein aggregation , biochemistry , alzheimer's disease , microtubule , biology , molecule , medicine , disease , gene , pathology , inorganic chemistry , physics , organic chemistry , quantum mechanics
Although the exact etiology and pathogenesis of Alzheimer's disease (AD) are still unclear, amyloid‐β (Aβ) generated by the proteolytic processing of amyloid‐β precursor protein (APP) aggregate to form toxic amyloid species. Kinesin‐1 is the first identified ATP‐dependent axonal transport motor protein that has been proven to affect Aβ generation and deposition. In this paper, we applied dual‐color fluorescence cross‐correlation spectroscopy (DC‐FCCS) to investigate the direct interaction of Aβ with kinesin‐1 at the single‐molecule fluorescence level in vitro . The results showed that two kinds of enhanced green fluorescent protein (EGFP)‐tagged kinesin light‐chain subunits of kinesin‐1(KLCs), KLC‐E and E‐KLC inhibited the aggregation of Aβ over a period of time, providing additional insight into the mechanism of axonal transport deficits in AD.