Abstract
The accumulation of β-amyloid peptide (Aβ) in the human brain is known to be the major cause that drives Alzheimer's disease pathogenesis. Aβ, a 39-42 amino acid peptide, is the cleavage product of amyloid precusor protein in the hydrophobic transmembrane region. The present study employs a two-dimensional (2D) approach. Two synthetic peptidolipids, C 18-IIGLM-OH and C 18-IIGLM-NH 2, are selected based on the fragment 31-35 of Aβ which is recognized as one of the determining segments that induces formation of amyloid fibril plaques. The aliphatic hydrocarbon chain C 18 is attached to the N-terminal of the fragment 31-35 to facilitate the 2D study at the air-water interface. The aggregation process is observed by two measurements: (1) surface pressure-area and surface dipole moment-area isotherms and (2) epifluorescence microscopy of the Langmuir films to investigate the topography of the amyloid-like formation.
Original language | English (US) |
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Pages (from-to) | 8641-8645 |
Number of pages | 5 |
Journal | Langmuir |
Volume | 20 |
Issue number | 20 |
DOIs | |
State | Published - Sep 28 2004 |
ASJC Scopus subject areas
- Materials Science(all)
- Condensed Matter Physics
- Surfaces and Interfaces
- Spectroscopy
- Electrochemistry