Phospholipid-induced fibrillation of a prion amyloidogenic determinant at the air /water interface

Jerzy Dorosz, Roman Volinsky, Ehud Bazar, Sofiya Kolusheva, Raz Jelinek

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The peptide fragment 106-126 of prion protein [PrP(106-126)] is a prominent amyloidogenic determinant. We present analysis of PrP(106-126) fibrillation at the air/water interface and, in particular, the relationship between the fibrillation process and interactions of the peptide with phospholipid monolayers. We find that lipid monolayers deposited at the air/water interface induce rapid formation of remarkably highly ordered fibrils by PrP(106-126), and that the extent of fibrillation and fiber organization were dependent upon the presence of negatively charged and unsaturated phospholipids in the monolayers. We also observe that fibrillation was enhanced when PrP(106-126) was injected underneath preassembled phospholipid monolayers, compared to deposition and subsequent compression of mixed monolayers of the peptide and phospholipids. In a broader context, this study demonstrates that Langmuir systems constitute a useful platform for studying lipid interactions of amyloidogenic peptides and lipid-induced fibrillation phenomena.

Original languageEnglish
Pages (from-to)12501-12506
Number of pages6
JournalLangmuir
Volume25
Issue number21
DOIs
StatePublished - 3 Nov 2009

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