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

Jiqian Wang*, Kai Tao, Peng Zhou, Elias Pambou, Zongyi Li, Hai Xu, Sarah Rogers, Stephen King, Jian R. Lu

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The effects of the two phenylalanine (Phe) residues in the blocked Aβ(16–22) peptide on its self-assembly have been investigated by replacing both of them with two cyclohexylalanines (Chas) or two phenylglycines (Phgs). TEM and SANS studies revealed that the flat and wide nanoribbons of Aβ(16–22) were transformed into thin nanotubes when replaced with Chas, and thinner and twisted nanofibrils when replaced with Phgs. The red-shifting degree of characteristic CD peaks suggested an increased twisting in the self-assembly of the derivative peptides, especially in the case of Ac-KLV(Phg)(Phg)AE-NH2. Furthermore, molecular dynamics (MD) simulations also indicated the increasing trend in twisting when Chas or Phgs were substituted for Phes. These results demonstrated that the hydrophobic interactions and spatial conformation between Cha residues were sufficient to cause lateral association of β-sheets to twisted/helical nanoribbons, which finally developed into nanotubes, while for Phg residue, the loss of the rotational freedom of the aromatic ring induced much stronger steric hindrance for the lateral stacking of Ac-KLV(Phg)(Phg)AE-NH2 β-sheets, eventually leading to the nanofibril formation. This study thus demonstrates that both the aromatic structure and the steric conformation of Phe residues are crucial in Aβ(16–22) self-assembly, especially in the significant lateral association of β-sheets.

Original languageEnglish
Pages (from-to)116-123
Number of pages8
JournalColloids and Surfaces B: Biointerfaces
StatePublished - 1 Nov 2016
Externally publishedYes


  • Amyloid peptides
  • Aromatic interaction
  • Morphology
  • Self-assembly
  • Steric hindrance


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