Abstract
The neuritic plaques formed by amyloid β-peptide (Aβ) play a seminal role in the pathogenesis of Alzheimer's disease (AD). Aβ sequence 25-35 (GSNKGAIIGLM) is among the most frequently studied Aβ derivatives for the reason that it possesses the structural characteristic of Aβ and remains neurotoxic. Aβ(25-35) was modified with an aliphatic chain (C 18) at the N-terminal of the peptide for the study of the Langmuir monolayer at the air-water interface. The main advantage of the 2D approach is the self-assembly of the peptide moiety in the subphase, and therefore the aggregation process of the peptidolipid Aβ(25-35) was monitored by surface pressure and surface potential-area isotherms. The real-time epifluorescence microscopy was utilized to observe the topography of the domains formed, whereas polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) provided the information on the structural features of the domains at the air-water interface. Langmuir-Blodgett films were prepared to examine by circular dichroism (CD) the conformation of the peptidolipid film in the domains.
| Original language | English |
|---|---|
| Pages (from-to) | 4661-4666 |
| Number of pages | 6 |
| Journal | Journal of Physical Chemistry C |
| Volume | 111 |
| Issue number | 12 |
| DOIs | |
| State | Published - Mar 29 2007 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Energy(all)
Cite this
A two-dimensional approach to study amyloid β-peptide fragment (25-35). / Triulzi, Robert C.; Li, Changqing; Naistat, David; Orbulescu, Jhony; Leblanc, Roger.
In: Journal of Physical Chemistry C, Vol. 111, No. 12, 29.03.2007, p. 4661-4666.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A two-dimensional approach to study amyloid β-peptide fragment (25-35)
AU - Triulzi, Robert C.
AU - Li, Changqing
AU - Naistat, David
AU - Orbulescu, Jhony
AU - Leblanc, Roger
PY - 2007/3/29
Y1 - 2007/3/29
N2 - The neuritic plaques formed by amyloid β-peptide (Aβ) play a seminal role in the pathogenesis of Alzheimer's disease (AD). Aβ sequence 25-35 (GSNKGAIIGLM) is among the most frequently studied Aβ derivatives for the reason that it possesses the structural characteristic of Aβ and remains neurotoxic. Aβ(25-35) was modified with an aliphatic chain (C 18) at the N-terminal of the peptide for the study of the Langmuir monolayer at the air-water interface. The main advantage of the 2D approach is the self-assembly of the peptide moiety in the subphase, and therefore the aggregation process of the peptidolipid Aβ(25-35) was monitored by surface pressure and surface potential-area isotherms. The real-time epifluorescence microscopy was utilized to observe the topography of the domains formed, whereas polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) provided the information on the structural features of the domains at the air-water interface. Langmuir-Blodgett films were prepared to examine by circular dichroism (CD) the conformation of the peptidolipid film in the domains.
AB - The neuritic plaques formed by amyloid β-peptide (Aβ) play a seminal role in the pathogenesis of Alzheimer's disease (AD). Aβ sequence 25-35 (GSNKGAIIGLM) is among the most frequently studied Aβ derivatives for the reason that it possesses the structural characteristic of Aβ and remains neurotoxic. Aβ(25-35) was modified with an aliphatic chain (C 18) at the N-terminal of the peptide for the study of the Langmuir monolayer at the air-water interface. The main advantage of the 2D approach is the self-assembly of the peptide moiety in the subphase, and therefore the aggregation process of the peptidolipid Aβ(25-35) was monitored by surface pressure and surface potential-area isotherms. The real-time epifluorescence microscopy was utilized to observe the topography of the domains formed, whereas polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) provided the information on the structural features of the domains at the air-water interface. Langmuir-Blodgett films were prepared to examine by circular dichroism (CD) the conformation of the peptidolipid film in the domains.
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UR - http://www.scopus.com/inward/citedby.url?scp=34147173268&partnerID=8YFLogxK
U2 - 10.1021/jp0669005
DO - 10.1021/jp0669005
M3 - Article
AN - SCOPUS:34147173268
VL - 111
SP - 4661
EP - 4666
JO - Journal of Physical Chemistry C
JF - Journal of Physical Chemistry C
SN - 1932-7447
IS - 12
ER -