The conformation of the Congo-red ligand bound to amyloid fibrils 
HET-s(218–289): a solid-state NMR study

Gowda, Chandrakala; Zandomeneghi, Giorgia; Zimmermann, Herbert; Schütz, Anne K.; Böckmann, Anja; Ernst, Matthias; Meier, Beat H.

doi:10.1007/s10858-017-0148-z

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The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study

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Zimmermann, Herbert
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Gowda, C., Zandomeneghi, G., Zimmermann, H., Schütz, A. K., Böckmann, A., Ernst, M., et al. (2017). The conformation of the Congo-red ligand bound to amyloid fibrils HET-s(218–289): a solid-state NMR study. Journal of Biomolecular NMR, 69(4), 207-213. doi:10.1007/s10858-017-0148-z.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002E-2349-D

Zusammenfassung

We have previously shown that Congo red (CR) binds site specifically to amyloid fibrils formed by HET-s(218–289) with the long axis of the CR molecule almost parallel to the fibril axis. HADDOCK docking studies indicated that CR adopts a roughly planar conformation with the torsion angle ϕ characterizing the relative orientation of the two phenyl rings being a few degrees. In this study, we experimentally determine the torsion angle ϕ at the center of the CR molecule when bound to HET-s(218–289) amyloid fibrils using solid-state NMR tensor-correlation experiments. The method described here relies on the site-specific 13C labeling of CR and on the analysis of the two-dimensional magic-angle spinning tensor-correlation spectrum of 13C2-CR. We determined the torsion angle ϕ to be 19°.