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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.…
Autor*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 |
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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: | Chemie und Prozesstechnik |
Chemie und Prozesstechnik / Chemische Charakterisierung und Spurenanalytik | |
DOI: | 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): | Creative 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 |