Measurements of residual dipolar couplings in peptide inhibitors weakly aligned by transient binding to peptide amyloid fibrils

Journal of Biomolecular NMR
Zhongjing Chen, Bernd Reif

Abstract

In this communication, we suggest that transferred residual dipolar couplings (trRDCs) can be employed to restrain the structure of peptide inhibitors transiently binding to beta-amyloid fibrils. The effect is based on the spontaneous alignment of amyloid fibrils with the fibril axis parallel to the magnetic field. This alignment is transferred to the transiently binding peptide inhibitor and is reflected in the size of the trRDCs. We find that the peptide inhibitor adopts a beta-sheet conformation with the backbone N-H and C-H dipolar vectors aligned preferentially parallel and perpendicular, respectively, to the fibril axis.

Citations

Mar 28, 2007·Journal of the American Chemical Society·Ronald D SeidelJames H Prestegard
Feb 4, 2012·Journal of Molecular Biology·Juan Miguel Lopez del AmoBernd Reif
Oct 23, 2008·Magnetic Resonance in Chemistry : MRC·Vladimir V KlochkovStefan Berger
Feb 20, 2008·Chembiochem : a European Journal of Chemical Biology·Anasztázia HetényiBotond Penke
Apr 17, 2008·Protein Science : a Publication of the Protein Society·Tiandi ZhuangJames H Prestegard
Nov 8, 2005·Journal of Molecular Biology·Zhongjing ChenBernd Reif

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