Amyloid-like formation by self-assembly of peptidolipids in two dimensions

Changqing Li, Jhony Orbulescu, Guodong Sui, Roger M. Leblanc

Research output: Contribution to journalArticle

21 Scopus citations

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 languageEnglish (US)
Pages (from-to)8641-8645
Number of pages5
JournalLangmuir
Volume20
Issue number20
DOIs
StatePublished - Sep 28 2004

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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