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

  • 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. WhereasAmyloid 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.zeige mehrzeige weniger

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Metadaten
Autoren/innen:M. Santos de Freitas, R. R. Araghi, E. Brandenburg, Jork Leiterer, Franziska EmmerlingORCiD, K. Folmert, U. I. M. Gerling-Driessen, B. Bardiaux, C. Böttcher, K. Pagel, A. Diehl, H. v. Berlepsch, H. Oschkinat, B. Koksch
Dokumenttyp:Zeitschriftenartikel
Veröffentlichungsform:Verlagsliteratur
Sprache:Englisch
Titel des übergeordneten Werkes (Englisch):Journal of Structural Biology
Jahr der Erstveröffentlichung:2018
Organisationseinheit der BAM:6 Materialchemie
6 Materialchemie / 6.3 Strukturanalytik
Veröffentlichende Institution:Bundesanstalt für Materialforschung und -prüfung (BAM)
Verlag:Elsevier
Jahrgang/Band:203
Ausgabe/Heft:3
Erste Seite:263
Letzte Seite:272
DDC-Klassifikation:Naturwissenschaften und Mathematik / Chemie / Analytische Chemie
Freie Schlagwörter:Elektronenmikroskopie
Amyloid
Themenfelder/Aktivitätsfelder der BAM:Analytical Sciences
Analytical Sciences / Spurenanalytik und chemische Zusammensetzung
DOI:https://doi.org/10.1016/j.jsb.2018.05.009
URN:urn:nbn:de:kobv:b43-458713
URL:https://www.sciencedirect.com/science/article/pii/S1047847718301333
ISSN:1047-8477
Verfügbarkeit des Dokuments:Datei für die Öffentlichkeit verfügbar ("Open Access")
Lizenz (Deutsch):License LogoCreative Commons - CC BY-NC-ND - Namensnennung - Nicht kommerziell - Keine Bearbeitungen 4.0 International
Datum der Freischaltung:07.09.2018
Referierte Publikation:Ja
Datum der Eintragung als referierte Publikation:07.09.2018
Schriftenreihen ohne Nummerierung:Wissenschaftliche Artikel der BAM