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Experimental Genetics Group
Neurobiol Aging. 2008 Nov 21.[Epub ahead of print] Larbanoix L1, Burtea C1, Laurent S1, Van Leuven F2, Toubeau G3, Elst LV1, Muller RN1*. 1Department of General, Organic and Biomedical Chemistry, NMR and Molecular Imaging Laboratory, University of Mons-Hainaut, Mons, Belgium. 2Experimental Genetics Group, KULEuven, Leuven, Belgium. 3Department of Histology, University of Mons-Hainaut, Mons, Belgium. *Corresponding author. 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 (Abeta(42)). A random disulfide constrained heptapeptide phage display library was screened against Abeta(42). After biopanning, 72 phage clones were isolated and their binding affinity to Abeta(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 Abeta(42) are in the picomolar range. The binding affinity for Abeta(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 Abeta(42) were identified by phage display. As specific carriers, they have a real potential for molecular imaging of AD thanks to AP binding.  FULL TEXT |
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