title: 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.
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Carolin
authors.initials: C
authors.lastname: Seuring
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Julia
authors.initials: J
authors.lastname: Gath
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Joeri
authors.initials: J
authors.lastname: Verasdonck
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Riccardo
authors.initials: R
authors.lastname: Cadalbert
authors.affiliation: Structural Biology Laboratory, The Salk Institute, 10010 N Torrey Pines Road, La Jolla, CA, 92037, USA.
authors.forename: Jean
authors.initials: J
authors.lastname: Rivier
authors.affiliation: Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France.
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland.
authors.forename: Beat H
authors.initials: BH
authors.lastname: Meier
authors.affiliation: Laboratory of Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland. roland.riek@phys.chem.ethz.ch.|Structural Biology Laboratory, The Salk Institute, 10010 N Torrey Pines Road, La Jolla, CA, 92037, USA. roland.riek@phys.chem.ethz.ch.
authors.forename: Roland
authors.initials: R
authors.lastname: Riek
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072757:Protein Conformation, beta-Strand; D055503:Protein Multimerization; D016415:Sequence Alignment; D001615:beta-Endorphin / Q000737:chemistry*
chemical_list: D000682:Amyloid; D001615:beta-Endorphin
keywords: Assignment; Functional amyloid; Secondary structure; Solid-state NMR; β-endorphin fibrils; β-strand