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 |
|---|---|
| Pages (from-to) | 8641-8645 |
| Number of pages | 5 |
| Journal | Langmuir |
| Volume | 20 |
| Issue number | 20 |
| DOIs | |
| State | Published - Sep 28 2004 |
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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 journal › Article
}
TY - JOUR
T1 - Amyloid-like formation by self-assembly of peptidolipids in two dimensions
AU - Li, Changqing
AU - Orbulescu, Jhony
AU - Sui, Guodong
AU - Leblanc, Roger
PY - 2004/9/28
Y1 - 2004/9/28
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=5444228433&partnerID=8YFLogxK
U2 - 10.1021/la0490339
DO - 10.1021/la0490339
M3 - Article
C2 - 15379486
AN - SCOPUS:5444228433
VL - 20
SP - 8641
EP - 8645
JO - Langmuir
JF - Langmuir
SN - 0743-7463
IS - 20
ER -