NR AWYA
AU Wang,Y.; Goodson,T. 3rd
TI Early aggregation in prion peptide nanostructures investigated by nonlinear and ultrafast time-resolved fluorescence spectroscopy
QU The Journal of Physical Chemistry. B 2007 Jan 18; 111(2): 327-30
PT letter; research support, u.s. gov't, non-p.h.s.
AB We report the characterization of early aggregates in the self-assembly of prion peptides using nonlinear and ultrafast time-resolved fluorescence spectroscopy. The dye-labeled peptide and dye/peptide guest-host systems were used to demonstrate the feasibility of the new approach. By measuring the two-photon absorption cross-section, small aggregates of the dye labeled peptide were characterized. Ultrafast time-resolved fluorescence anisotropy spectroscopy reveals the packing state (microenvironment) of the probes to be tightly associated with aggregates and associated with aggregation progression of the peptides. Fluorescence intensity decay shows a correlation with growth of aggregates having a high level of structured beta-sheet content. A new binding ligand Cascade Yellow shows promise for beta-sheet recognition of prion peptide nanostructures. These findings may have implications for in vivo studies of neurotoxic aggregates targeting with fluorescence markers. Also, these results may provide insight into molecular design of peptide-based nanomaterials.
MH Coloring Agents/chemistry; Ligands; Nanostructures/*chemistry; Peptides/*chemistry; Prions/*chemistry; Sensitivity and Specificity; Spectrometry, Fluorescence/*methods; Time Factors
SP englisch
PO USA