Solid-state NMR sequential assignment of the β-endorphin peptide in its amyloid form
Abstract
Insights into the three-dimensional structure of hormone fibrils are crucial for a detailed understanding of how an amyloid structure allows the storage of hormones in secretory vesicles prior to hormone secretion into the blood stream. As an example for various hormone amyloids, we have studied the endogenous opioid neuropeptide β-endorphin in one of its fibril forms. We have achieved the sequential assignment of the chemical shifts of the backbone and side-chain heavy atoms of the fibril. The secondary chemical shift analysis revealed that the β-endorphin peptide adopts three β-strands in its fibril state. This finding fosters the amyloid nature of a hormone at the atomic level. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000116540Publication status
publishedExternal links
Journal / series
Biomolecular NMR AssignmentsVolume
Pages / Article No.
Publisher
SpringerSubject
β-endorphin fibrils; Functional amyloid; Solid-state NMR; Assignment; Secondary structure; β-strandOrganisational unit
03782 - Riek, Roland / Riek, Roland
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
Notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.More
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