Abstract
A10K (A=alanine, K=lysine) model peptides self-assemble into ribbon-like β-sheet aggregates. Here, we report an X-ray diffraction investigation on a flow-aligned dispersion of these self-assembly structures. The two-dimensional wide-angle X-ray scattering pattern suggests that peptide pack in a two-dimensional oblique lattice, essentially identical to the crystalline packing of polyalanine, An (for n>4). One side of the oblique unit cell, corresponding to the anti-parallel β-sheet, is oriented along the ribbon's axis. Together with recently published small angle X-ray scattering data of the same system, this work thus yields a detailed description of the self-assembled ribbon aggregates, down to the molecular length scale. Notably, our results highlight the importance of the crystalline peptide packing within its self-assembly aggregates, which is often neglected.
Original language | English |
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Pages (from-to) | 1519-1523 |
Number of pages | 5 |
Journal | ChemPhysChem |
Volume | 21 |
Issue number | 14 |
DOIs | |
Publication status | Published - 2020 Jul 17 |
Subject classification (UKÄ)
- Physical Chemistry
Keywords
- aggregation
- flow alignment
- peptides
- structure elucidation
- X-ray diffraction