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• W2023621718 endingPage "15201" @default.
• W2023621718 startingPage "15195" @default.
• W2023621718 abstract "The aggregation of amyloid beta-peptide (Abeta(1-40)) into fibrils is a key pathological process associated with Alzheimer's disease. This work has investigated the micellization process of biosurfactant surfactin and its effect on the aggregation behavior of Abeta(1-40). The results show that surfactin has strong self-assembly ability to form micelles and the micelles tend to form larger aggregates. Surfactin adopts a beta-turn conformation at low micelle concentration but a beta-sheet conformation at high micelle concentration. The effect of surfactin on the Abeta(1-40) aggregation behavior exhibits a strong concentration-dependent fashion. Below the critical micelle concentration of surfactin, the electrostatic binding of surfactin monomers on Abeta(1-40) causes Abeta(1-40) molecules to unfold. Assisted by the hydrophobic interaction among surfactin monomers on the Abeta(1-40) chain, the conformation of Abeta(1-40) transfers to the beta-sheet structure, which promotes the formation of fibrils. At low surfactin micelle concentration, besides the electrostatic force and hydrophobic interaction, hydrogen bonds formed between surfactin micelles and adjacent Abeta(1-40) peptide chains may promote the ordered organization of these Abeta(1-40) peptide chains, thus leading to the formation of beta-sheets and fibrils to a great extent. At high surfactin micelle concentration, the separating of Abeta(1-40) chains by the excessive surfactin micelles and the aggregation of the complexes of Abeta(1-40) with surfactin micelles inhibit the formation of beta-sheets and fibrils." @default.
• W2023621718 created "2016-06-24" @default.
• W2023621718 creator A5028883593 @default.
• W2023621718 creator A5054617946 @default.
• W2023621718 creator A5056361433 @default.
• W2023621718 creator A5082549798 @default.
• W2023621718 date "2008-11-05" @default.
• W2023621718 modified "2023-09-27" @default.
• W2023621718 title "Micellization of Surfactin and Its Effect on the Aggregate Conformation of Amyloid β(1-40)" @default.
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• W2023621718 doi "https://doi.org/10.1021/jp805966x" @default.
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• W2023621718 hasPublicationYear "2008" @default.
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