期刊
RSC ADVANCES
卷 10, 期 49, 页码 29510-29515出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0ra04480f
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资金
- Ministry of Science and Technology, Taiwan [103-2113-M-002-013-MY3]
- Ministry of Science and Technology
- Chien
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 surfaceviathe diffusion-limited aggregation process.
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