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2010-10-31 - Article/Dans un journal avec peer-review - Anglais - 10 page(s)

Larbanoix Lionel , Burtea Carmen , Laurent Sophie , Van Leuven Fred, Toubeau Gérard, Vander Elst Luce , Muller Robert , "Potential amyloid plaque-specific peptides for the diagnosis of Alzheimer's disease" in Neurobiology of Aging, 31, 10, 1679-89

  • Edition : Elsevier (Netherlands)
  • Codes CREF : Sciences biomédicales (DI3200), Biologie moléculaire (DI3111), Imagerie médicale, radiologie, tomographie (DI3243)
  • Unités de recherche UMONS : Chimie générale, organique et biomédicale (M108), Histologie (M118)
  • Instituts UMONS : Institut des Sciences et Technologies de la Santé (Santé)
Texte intégral :

Abstract(s) :

(Anglais) Amyloid plaques (AP) represent one of the main molecular hallmarks of Alzheimer's disease (AD). In order to develop new AP-specific contrast agents for AD molecular imaging, the phage display technology was used to identify peptides specific to amyloid-beta (A beta(42)). A random disulfide constrained heptapeptide phage display library was screened against A beta(42). After biopanning, 72 phage clones were isolated and their binding affinity to A beta(42) was evaluated by enzyme-linked immunosorbent assay (ELISA). The final library was enriched in two peptide sequences. The K(d) of candidate phage clones for binding to A beta(42) are in the picomolar range. The binding affinity for A beta(42) of two selected peptides was confirmed by ELISA, and the specific interaction with AP was validated by immunohistochemistry on brain sections. The preliminary MRI in vivo study, which was performed with a peptide functionalized contrast agent on AD transgenic mouse, showed encouraging results. To conclude, low molecular weight peptides presenting a specific affinity for A beta(42) were identified by phage display. As specific carriers, they have a real potential for molecular imaging of AD thanks to AP binding.

Identifiants :
  • DOI : 10.1016/j.neurobiolaging.2008.09.021