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Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate

Kuczera, Stefan LU ; Rüter, Axel LU orcid ; Roger, Kevin LU and Olsson, Ulf LU orcid (2020) In ChemPhysChem 21(14). p.1519-1523
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,... (More)

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.

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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
aggregation, flow alignment, peptides, structure elucidation, X-ray diffraction
in
ChemPhysChem
volume
21
issue
14
pages
5 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:85087138071
  • pmid:32573909
ISSN
1439-4235
DOI
10.1002/cphc.201901126
language
English
LU publication?
yes
id
876ac00e-1cdc-4b39-b6a7-2b0daba16195
date added to LUP
2020-11-03 12:51:46
date last changed
2025-10-14 11:30:47
@article{876ac00e-1cdc-4b39-b6a7-2b0daba16195,
  abstract     = {{<p>A<sub>10</sub>K (A=alanine, K=lysine) model peptides self-assemble into ribbon-like <i>β</i>-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, A<sub>n</sub> (for <i>n</i>&gt;4). One side of the oblique unit cell, corresponding to the anti-parallel <i>β</i>-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.</p>}},
  author       = {{Kuczera, Stefan and Rüter, Axel and Roger, Kevin and Olsson, Ulf}},
  issn         = {{1439-4235}},
  keywords     = {{aggregation; flow alignment; peptides; structure elucidation; X-ray diffraction}},
  language     = {{eng}},
  month        = {{07}},
  number       = {{14}},
  pages        = {{1519--1523}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{ChemPhysChem}},
  title        = {{Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate}},
  url          = {{http://dx.doi.org/10.1002/cphc.201901126}},
  doi          = {{10.1002/cphc.201901126}},
  volume       = {{21}},
  year         = {{2020}},
}