Manifold of self-assembly of a de novo designed peptide: amyloid fibrils, peptide bundles, and fractals.

Autor:	Chao YJ; Department of Chemistry, National Taiwan University No. 1, Section 4, Roosevelt Road Taipei 10617 Taiwan chanjcc@ntu.edu.tw., Wu K; Department of Chemistry, National Taiwan University No. 1, Section 4, Roosevelt Road Taipei 10617 Taiwan chanjcc@ntu.edu.tw., Chang HH; Department of Chemistry, National Taiwan University No. 1, Section 4, Roosevelt Road Taipei 10617 Taiwan chanjcc@ntu.edu.tw., Chien MJ; Department of Chemistry, National Taiwan University No. 1, Section 4, Roosevelt Road Taipei 10617 Taiwan chanjcc@ntu.edu.tw., Chan JCC; Department of Chemistry, National Taiwan University No. 1, Section 4, Roosevelt Road Taipei 10617 Taiwan chanjcc@ntu.edu.tw.
Jazyk:	angličtina
Zdroj:	RSC advances [RSC Adv] 2020 Aug 10; Vol. 10 (49), pp. 29510-29515. Date of Electronic Publication: 2020 Aug 10 (Print Publication: 2020).
DOI:	10.1039/d0ra04480f
Abstrakt:	We report that a peptide with the sequence of EGAGAAAAGAGE can have different aggregation states, viz. , amyloid fibrils, peptide bundles, and fractal assembly under different incubation conditions. The chemical state of the Glu residue played a pivotal regulating role in the aggregation behavior of the peptide. The mechanism of the fractal assembly of this peptide has been unraveled as follows. The peptide fragments adopting the beta-sheet conformation are well dispersed in alkaline solution. In the buffer of sodium bicarbonate, peptide rods are formed with considerable structural rigidity at the C- and N-termini. The peptide rods undergo random trajectory in the solution and form a fractal pattern on a two-dimensional surface via the diffusion-limited aggregation process. Competing Interests: There are no conflicts to declare. (This journal is © The Royal Society of Chemistry.)
Databáze:	MEDLINE
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