Tuning self-assembled morphology of the Aβ(16–22) peptide by substitution of phenylalanine residues

[Display omitted] •Hydrophobic interactions and steric conformation of Phes affect Aβ self-assembly.•When Phes replaced with Chas, Aβ(16–22) formed thin nanotubes morphologies.•When Phes replaced with Phgs, Aβ(16–22) formed thinner and twisted nanofibrils.•Equilibrium between lateral aggregation and...

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Veröffentlicht in:	Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2016-11, Vol.147, p.116-123
Hauptverfasser:	Wang, Jiqian, Tao, Kai, Zhou, Peng, Pambou, Elias, Li, Zongyi, Xu, Hai, Rogers, Sarah, King, Stephen, Lu, Jian R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Amyloid peptides Aromatic interaction Humans Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Microscopy, Atomic Force Microscopy, Electron, Transmission Molecular Dynamics Simulation Morphology Nanostructure Nanotubes Nanotubes - chemistry Peptides Phenylalanine Phenylalanine - chemistry Phenylalanine - metabolism Residues Scattering, Small Angle Self assembly Steric hindrance Tuning Twisting
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