Disassembly of Amyloid Fibrils by Premicellar and Micellar Aggregates of a Tetrameric Cationic Surfactant in Aqueous Solution

被引:23
作者
He, Chengqian [1 ]
Hou, Yanbo [1 ]
Han, Yuchun [1 ]
Wang, Yilin [1 ]
机构
[1] Chinese Acad Sci, Key Lab Colloid & Interface Sci, Beijing Natl Lab Mol Sci, Inst Chem, Beijing 100190, Peoples R China
基金
中国国家自然科学基金;
关键词
ALZHEIMERS-DISEASE; GEMINI SURFACTANT; ALPHA-SYNUCLEIN; FIBRILLOGENESIS; CYTOTOXICITY; INHIBITION; PARKINSONS; RIFAMPICIN; MECHANISM; DOPAMINE;
D O I
10.1021/la200350j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Vie report a finding that not only the micelles but also the premicellar aggregates of a star-like tetrameric quaternary ammonium surfactant PATC can disassemble and clear mature beta-amyloid A beta(1-40) fibrils in aqueous solution. Different from other surfactants, PATC self assembles into network-like aggregates below its critical micelle concentration (CMC). The strong self-assembly ability of PATC even below its CMC enable PATC to disaggregate the A beta(1-40) fibrils far below the Charge neutralization point of the A beta( 1-40) with PATC. There maybe two key features of the fibril disassembly induced by the surfactant First, the positively charged surfactant molecules bind with the negatively charged A beta(1-40) fibrils through electrostatic interaction. Second, the self assembly of the surfactant molecules bound onto the A beta(1-40) fibrils disaggregate the fibrils, and the surfactant molecules form mixed aggregates with the A beta(1-40) molecules. The result reveals a structural approach of constructing efficient disassembly agents to mature beta-amyloid fibrils.
引用
收藏
页码:4551 / 4556
页数:6
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