Thread: NMR paper Solid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.
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Default Solid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.
Solid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.

Related Articles Solid-state NMR sequential assignment of the ?-endorphin peptide in its amyloid form.

Biomol NMR Assign. 2016 Oct;10(2):259-68

Authors: Seuring C, Gath J, Verasdonck J, Cadalbert R, Rivier J, Böckmann A, Meier BH, Riek R

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 ?-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 ?-endorphin peptide adopts three ?-strands in its fibril state. This finding fosters the amyloid nature of a hormone at the atomic level.


PMID: 27165576 [PubMed - indexed for MEDLINE]



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