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

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

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Side-chains:

NOEs:

Structure from NMR restraints:

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GeNMR

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Amber

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Torsion angles from chemical shifts:

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Promega- Proline

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TALOS

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HADDOCK

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Camshift

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ArShift- Aromatic

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CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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11-01-2017, 07:49 PM

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

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

Abstract

We have previously shown that Congo red (CR) binds site specifically to amyloid fibrils formed by HET-s(218â??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 Ï? characterizing the relative orientation of the two phenyl rings being a few degrees. In this study, we experimentally determine the torsion angle Ï? at the center of the CR molecule when bound to HET-s(218â??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 Ï? to be 19Â°.

Source: Journal of Biomolecular NMR

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