Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate

Stefan Kuczera, Axel Rüter, Kevin Roger, Ulf Olsson

Research output: Contribution to journalArticlepeer-review

5 Citations (SciVal)

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 languageEnglish
Pages (from-to)1519-1523
Number of pages5
JournalChemPhysChem
Volume21
Issue number14
DOIs
Publication statusPublished - 2020 Jul 17

Subject classification (UKÄ)

  • Physical Chemistry

Keywords

  • aggregation
  • flow alignment
  • peptides
  • structure elucidation
  • X-ray diffraction

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