期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 420, 期 1, 页码 136-140出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.02.129
关键词
Conformation; Amyloid-beta peptide; Surfactants; Micelles; Sulfate monolayers; Electrostatic interactions; Hydrophobic effect
资金
- FCT [PTDC/QUI-BIQ/102827/2008]
- Fundação para a Ciência e a Tecnologia [PTDC/QUI-BIQ/102827/2008] Funding Source: FCT
The conformation of amyloid-beta peptide (A beta) determines if toxic aggregates are formed. The peptide structure by its turn depends on the environment and molecule-molecule interactions. We characterized the secondary structure of A beta-(1-40) in surfactant solutions and interacting with monolayers. The peptide adopts beta-sheet structure in solutions of ionic surfactants at sub-micelle concentrations and alpha-helix in the presence of ionic micelles. Uncharged micelles induce beta-sheets. A beta-(1-40) alters the critical micelle concentration value of the non-ionic surfactant, underlining hydrophobic interactions. At ionic monolayers the peptide forms beta-sheets when its concentration at the surface is high enough. These results suggest that only electrostatic interactions of charged micelles that surround completely the peptide are able to induce non-aggregated a-helix structure. (C) 2012 Elsevier Inc. All rights reserved.
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