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

Changqing Li, Jhony Orbulescu, Guodong Sui, Roger Leblanc

Research output: Contribution to journalArticle

20 Citations (Scopus)

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

Fingerprint

Amyloid
Self assembly
peptides
self assembly
fragments
aliphatic hydrocarbons
pathogenesis
Peptides
brain
amino acids
cleavage
topography
isotherms
dipole moments
Langmuir Blodgett films
Dipole moment
Hydrocarbons
microscopy
proteins
Topography

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Amyloid-like formation by self-assembly of peptidolipids in two dimensions. / Li, Changqing; Orbulescu, Jhony; Sui, Guodong; Leblanc, Roger.

In: Langmuir, Vol. 20, No. 20, 28.09.2004, p. 8641-8645.

Research output: Contribution to journalArticle

Li, Changqing ; Orbulescu, Jhony ; Sui, Guodong ; Leblanc, Roger. / Amyloid-like formation by self-assembly of peptidolipids in two dimensions. In: Langmuir. 2004 ; Vol. 20, No. 20. pp. 8641-8645.
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