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  • Title: Disassembly of amyloid fibrils by premicellar and micellar aggregates of a tetrameric cationic surfactant in aqueous solution.
    Author: He C, Hou Y, Han Y, Wang Y.
    Journal: Langmuir; 2011 Apr 19; 27(8):4551-6. PubMed ID: 21438511.
    Abstract:
    We 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 β-amyloid Aβ(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 enables PATC to disaggregate the Aβ(1-40) fibrils far below the charge neutralization point of the Aβ(1-40) with PATC. There may be two key features of the fibril disassembly induced by the surfactant. First, the positively charged surfactant molecules bind with the negatively charged Aβ(1-40) fibrils through electrostatic interaction. Second, the self-assembly of the surfactant molecules bound onto the Aβ(1-40) fibrils disaggregate the fibrils, and the surfactant molecules form mixed aggregates with the Aβ(1-40) molecules. The result reveals a structural approach of constructing efficient disassembly agents to mature β-amyloid fibrils.
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