Dioleoyl-phosphatidic acid selectively binds to α-synuclein and strongly induces its aggregation

Satoru Mizuno, Hirotaka Sasai, Aiko Kume, Daisuke Takahashi, Mamoru Satoh, Sayaka Kado, Fumio Sakane

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

α-Synuclein (α-syn), which causally links to Parkinson's disease, binds to vesicles containing phosphatidic acid (PA). However, the effects of the fatty acyl chains of PA on its ability to bind to α-syn protein remain unclear. Intriguingly, we reveal that among several PA species, 18:1/18:1-PA is the most strongly bound PA to the α-syn protein. Moreover, 18:1/18:1-PA more strongly enhances secondary structural changes from the random coil form to the α-helical form than 16:0/18:1-PA. Furthermore, 18:1/18:1-PA more markedly accelerates generation of multimeric and proteinase K-resistant α-syn protein compared to 16:0/18:1-PA. These results indicate that among phospholipids examined so far, 18:1/18:1-PA demonstrates the strongest binding to α-syn, as well as the most effective enhancement of its secondary structural changes and aggregation formation.

Original languageEnglish
Pages (from-to)784-791
Number of pages8
JournalFEBS Letters
Volume591
Issue number5
DOIs
Publication statusPublished - Mar 2017

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