Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
(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
- Kuczera, Stefan LU ; Rüter, Axel LU ; Roger, Kevin LU and Olsson, Ulf LU
- organization
- publishing date
- 2020-07-17
- 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
-
- pmid:32573909
- scopus:85087138071
- 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
- 2024-06-27 00:18:56
@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>>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}}, }