Evidence for the binding of phosphate ion to the C-terminus region in Aβ 1-40 using heteronuclear NMR analyses

Makiko Nagata-Uchiyama, Yoshito Abe, Akira Monji, Shigenobu Kanba, Tadashi Ueda

Research output: Contribution to journalArticlepeer-review

Abstract

Amyloid fibril formation of amyloid beta peptide 1-40 (Aβ 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 Aβ 1-40 using chemical shift perturbation analysis of hetero-nuclear NMR. In titration analysis of 15N-labeled Aβ 1-40 in the presence of 150 mM phosphate ion or 150 mM chloride ion, we identified the residues affected by these ions in Aβ 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 β-strand region in Aβ 1-40. Therefore, we suggested that phosphate ions interacted with the potential -strand region in Aβ 1-40 to be hard to form β-sheet in Aβ 1-40, resulting in retardation of the amyloid fibril formation.

Original languageEnglish
Pages (from-to)176-180
Number of pages5
JournalProtein and Peptide Letters
Volume17
Issue number2
DOIs
Publication statusPublished - 2010

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

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