Phosphatidylethanolamine accelerates aggregation of the amyloidogenic N-terminal fragment of apoA-I

Naoko Kurimitsu, Chiharu Mizuguchi, Kaho Fujita, Suzuno Taguchi, Takashi Ohgita, Kazuchika Nishitsuji, Toshinori Shimanouchi, Hiroyuki Saito

Research output: Contribution to journalArticle

Abstract

Membrane lipid composition is known to influence aggregation and fibril formation of many amyloidogenic proteins. Here, we found that phosphatidylethanolamine (PE) accelerates aggregation of the N-terminal 1‒83 fragment of an amyloidogenic G26R variant of apoA-I on lipid membranes. Circular dichroism and isothermal titration calorimetry measurements demonstrated that PE does not affect the α-helical structure and lipid binding property of apoA-I 1-83/G26R. Rather, fluorescence measurements indicated that PE induces more ordered lipid packing at the interfacial and acyl chain regions, providing more hydrophobic environments especially around the highly amyloidogenic regions in apoA-I on the membrane surface. These results suggest that PE promotes aggregation of the amyloidogenic N-terminal fragment of apoA-I on lipid membranes by inducing hydrophobic membrane environments.

Original languageEnglish
Pages (from-to)1443-1452
Number of pages10
JournalFEBS Letters
Volume594
Issue number9
DOIs
Publication statusPublished - May 1 2020

Keywords

  • amyloid fibril
  • apolipoprotein A-I
  • lipid membrane
  • phosphatidylethanolamine
  • sphingomyelin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Kurimitsu, N., Mizuguchi, C., Fujita, K., Taguchi, S., Ohgita, T., Nishitsuji, K., Shimanouchi, T., & Saito, H. (2020). Phosphatidylethanolamine accelerates aggregation of the amyloidogenic N-terminal fragment of apoA-I. FEBS Letters, 594(9), 1443-1452. https://doi.org/10.1002/1873-3468.13737