Solution conformations of a peptide containing the cytoplasmic domain sequence of the β amyloid precursor protein

Christopher D. Kroenke, Dorota Ziemnicka-Kotula, Jiliu Xu, Leszek Kotula, Arthur G. Palmer

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

The cytoplasmic domain of the β amyloid precursor protein (βAPP) may play a role in cellular events that lead to the secretion of the Aβ peptide, the major constituent of amyloid plaques found in the brains of individuals affected by Alzheimer's disease, by interacting with cellular factors involved in βAPP function or processing. In order to elucidate the structural basis of cytoplasmic domain activity, the conformations adopted in solution by a peptide containing the 47-residue C-terminal sequence of βAPP have been investigated by NMR and CD spectroscopy. The peptide does not have a stable tertiary structure, but local regions of the polypeptide chain populate defined conformations. In particular, the amino acid sequences TPEE and NPTY form type I reverse turns. These structured regions correspond to sequences within the cytoplasmic domain implicated in the biological activity of βAPP.

Original languageEnglish (US)
Pages (from-to)8145-8152
Number of pages8
JournalBiochemistry
Volume36
Issue number26
DOIs
StatePublished - Jul 1 1997

ASJC Scopus subject areas

  • Biochemistry

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