title: Phospholipid-induced fibrillation of a prion amyloidogenic determinant at the air/water interface.
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.
authors: Department of Chemistry and Ilse Katz Institute of Nanotechnology, Ben Gurion University, Beer Sheva 84105, Israel.
authors: Jerzy
authors: J
authors: Dorosz
authors: Roman
authors: R
authors: Volinsky
authors: Ehud
authors: E
authors: Bazar
authors: Sofiya
authors: S
authors: Kolusheva
authors: Raz
authors: R
authors: Jelinek
mesh_terms: D000388:Air; D000682:Amyloid / Q000737:chemistry*; D046529:Microscopy, Electron, Transmission; D010743:Phospholipids / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water
chemical_list: D000682:Amyloid; D010743:Phospholipids; D011328:Prions; D014867:Water