Evidence for the binding of phosphate ion to the C-terminus region in Abeta1-40 using heteronuclear NMR analyses.

Abstract

Amyloid fibril formation of amyloid beta peptide 1-40 (Abeta 1-40) was reported to be retarded in the presence of 150mM phosphate buffer at pH 7 [Monji, Ustumi, Ueda, Imoto, Yoshida, Hashioka, Tashiro and Tashiro, J. Neurochemistry, 77, 1425-1432 (2007)]. In order to elucidate the reason why phosphate ion retards the amyloid fibril formation, we examined the preferential binding sites of phosphate ion to Abeta 1-40 using chemical shift perturbation analysis of heteronuclear NMR. In titration analysis of (15)N-labeled Abeta1-40 in the presence of 150 mM phosphate ion or 150 mM chloride ion, we identified the residues affected by these ions in Abeta 1-40. As a result, we found the tendency that phosphate ion preferentially bound to some residues located on the C-terminus region where the region was reported to be the potential beta-strand region in Abeta1-40. Therefore, we suggested that phosphate ions interacted with the potential beta-strand region in Abeta1-40 to be hard to form beta-sheet in Abeta 1-40, resulting in retardation of the amyloid fibril formation.

Cite this paper

@article{NagataUchiyama2010EvidenceFT, title={Evidence for the binding of phosphate ion to the C-terminus region in Abeta1-40 using heteronuclear NMR analyses.}, author={Makiko Nagata-Uchiyama and Yoshito Abe and Akira Monji and Shigenobu Kanba and Tadashi Ueda}, journal={Protein and peptide letters}, year={2010}, volume={17 2}, pages={176-80} }