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Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate.

ABSTRACT: A10 K (A=alanine, K=lysine) model peptides self-assemble into ribbon-like ?-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 ?-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.

SUBMITTER: Kuczera S

PROVIDER: S-EPMC7496194 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate.

Kuczera Stefan S Rüter Axel A Roger Kevin K Olsson Ulf U

Chemphyschem : a European journal of chemical physics and physical chemistry 20200623 14

A<sub>10</sub> K (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, A<sub>n</sub> (for n>4). One side of the oblique unit cell, corresponding to the anti-parallel ...[more]

PMID: 32573909

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