期刊
FEBS LETTERS
卷 586, 期 2, 页码 186-190出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.12.017
关键词
Protein aggregation; Supramolecular structure; Amphiphilic peptide; Dynamic light scattering; Electron microscopy
资金
- Presidium of the Russian Academy of Sciences
- Russian Foundation for Basic Research [11-04-00932-a]
A striking potential of the amphiphilic dipeptides, Arg-Phe or Asp-Phe, to induce aggregation of a model protein, alcohol dehydrogenase in its native-like state, has been demonstrated under physiologically relevant conditions, using dynamic light scattering, fluorescence spectroscopy, circular dichroism, transmission electron-and atomic force microscopy. The peptide action resulted in accumulation of a variety of morphologically distinct supramolecular structures profoundly differing from those generated by the heat-induced aggregation at the early stages of the process, when amyloid fibril assemblies were not detectable. The biogenic amphiphilic agents are suggested to act as regulators of structural transformations of native-like proteins. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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