The protofilament architecture of a de novo designed coiled coil-based amyloidogenic peptide

Autor: Beate Koksch, Benjamin Bardiaux, Hartmut Oschkinat, Hans von Berlepsch, Anne Diehl, Mônica S. Freitas, Franziska Emmerling, Jork Leiterer, Enrico Brandenburg, Kristin Folmert, Ulla I. M. Gerling-Driessen, Christoph Böttcher, Raheleh Rezaei Araghi, Kevin Pagel
Přispěvatelé: Freie Universität Berlin, Universidade Federal do Rio de Janeiro (UFRJ), Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] (FMP), Leibniz Association, BAM Federal Institute for Materials Research and Testing, Federal Institute for Materials Research and Testing - Bundesanstalt für Materialforschung und -prüfung (BAM), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Alexander von Humboldt Foundation Georg Forster Research Fellowship and by the CAPES-DAAD Bilateral Exchange of Academics (both awarded to M.S.F.), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2018
Předmět:
0301 basic medicine
Amyloid
Materials science
[SDV]Life Sciences [q-bio]
MESH: Protein Structure
Secondary
Amyloidogenic Proteins
Peptide
MESH: Amino Acid Sequence
Microscopy
Atomic Force
010402 general chemistry
01 natural sciences
Protein Structure
Secondary
law.invention
03 medical and health sciences
Protein Domains
Alzheimer Disease
Structural Biology
law
MESH: Nuclear Magnetic Resonance
Biomolecular
Electron microscopy
Humans
Amino Acid Sequence
Nuclear Magnetic Resonance
Biomolecular
Amyloid fibrils
MESH: Microscopy
Atomic Force
chemistry.chemical_classification
Coiled coil
MESH: Amyloid
MESH: Amyloidogenic Proteins
MESH: Humans
MESH: Peptides
Scattering
Cryoelectron Microscopy
Polymer
0104 chemical sciences
030104 developmental biology
chemistry
Transmission electron microscopy
Biophysics
MESH: Protein Domains
Substructure
MESH: Cryoelectron Microscopy
Electron microscope
Peptides
MESH: Alzheimer Disease
Zdroj: Journal of Structural Biology
Journal of Structural Biology, 2018, 203 (3), pp.263-272. ⟨10.1016/j.jsb.2018.05.009⟩
Journal of Structural Biology, Elsevier, 2018, 203 (3), pp.263-272. ⟨10.1016/j.jsb.2018.05.009⟩
ISSN: 1047-8477
1095-8657
Popis: International audience; Amyloid fibrils are polymers formed by proteins under specific conditions and in many cases they are related to pathogenesis, such as Parkinson's and Alzheimer's diseases. Their hallmark is the presence of a β-sheet structure. High resolution structural data on these systems as well as information gathered from multiple complementary analytical techniques is needed, from both a fundamental and a pharmaceutical perspective. Here, a previously reported de novo designed, pH-switchable coiled coil-based peptide that undergoes structural transitions resulting in fibril formation under physiological conditions has been exhaustively characterized by transmission electron microscopy (TEM), cryo-TEM, atomic force microscopy (AFM), wide-angle X-ray scattering (WAXS) and solid-state NMR (ssNMR). Overall, a unique 2-dimensional carpet-like assembly composed of large coexisiting ribbon-like, tubular and funnel-like structures with a clearly resolved protofilament substructure is observed. Whereas electron microscopy and scattering data point somewhat more to a hairpin model of β-fibrils, ssNMR data obtained from samples with selectively labelled peptides are in agreement with both, hairpin structures and linear arrangements.
Databáze: OpenAIRE
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