Surface chemistry of Alzheimer's disease

A Langmuir monolayer approach

Garima Thakur, Miodrag Micic, Roger Leblanc

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Amyloid beta (1-40) and (1-42) peptides are the major constituents of hallmark senile plaques found in Alzheimer's disease (AD) patients. Study of aggregation of Aβ (1-40) and (1-42) peptides and the truncated Aβ fragments could lead towards the mechanism of AD. Langmuir monolayer approach is one of the excellent methods to investigate the mechanism and origin of AD. Particularly, to study the steps involved in the formation and assembly of β-sheet structures leading to formation of amyloid fibrils. Surface pressure- and surface potential-area isotherms provide information regarding the nature of short-range and long-range interactions between the molecules especially the lipids and the Aβ peptides. Spectroscopic methods like IRRAS, PM-IRRAS, FTIR-ATR, and GIXD at the air-water interface provide insight into the structural characterization, and orientation of the molecules in the Langmuir monolayer.

Original languageEnglish
Pages (from-to)436-456
Number of pages21
JournalColloids and Surfaces B: Biointerfaces
Volume74
Issue number2
DOIs
StatePublished - Dec 1 2009

Fingerprint

monomolecular films
Surface chemistry
Peptides
peptides
Monolayers
Alzheimer Disease
chemistry
Lipid A
Molecules
Amyloid Plaques
Surface potential
Fourier Transform Infrared Spectroscopy
Amyloid
Lipids
Isotherms
lipids
molecules
isotherms
Agglomeration
assembly

Keywords

  • Alzheimer's disease
  • Amyloid beta
  • Langmuir monolayer
  • Surface chemistry

ASJC Scopus subject areas

  • Biotechnology
  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

Cite this

Surface chemistry of Alzheimer's disease : A Langmuir monolayer approach. / Thakur, Garima; Micic, Miodrag; Leblanc, Roger.

In: Colloids and Surfaces B: Biointerfaces, Vol. 74, No. 2, 01.12.2009, p. 436-456.

Research output: Contribution to journalArticle

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