In vitro perturbation of aggregation processes in beta-amyloid peptides: a spectroscopic study.
We have performed an in vitro study to investigate the molecular basis of the aggregation kinetic of 1-40 beta-amyloid peptides (Abeta and the possibility of affecting this aggregation process using an exogenous natural polycyclic pigment, hypericin (Hyp). The effect of Hyp on the self-assembly process at different times of the aggregation kinetic has been investigated utilizing a chaperon-like molecule, alpha-crystallin. Circular dichroism and fluorescence results suggest that Hyp can associate to precursors of the mature fibrils and perturb the aggregation process through intermolecular interactions with the Abeta peptides.
Sgarbossa
Antonella
A
Istituto di Biofisica del CNR, Unità di Pisa, Via G. Moruzzi 1, 56100 Pisa, Italy. antonella.sgarbossa@pi.ibf.cnr.it
Buselli
Dario
D
Lenci
Francesco
F
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D000873:Anthracenes; D002942:Circular Dichroism; D005456:Fluorescent Dyes / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry*; D010569:Perylene / Q000031:analogs & derivatives* / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D038201:alpha-Crystallins / Q000737:chemistry*
D016229:Amyloid beta-Peptides; D000873:Anthracenes; D005456:Fluorescent Dyes; D010446:Peptide Fragments; D038201:alpha-Crystallins; C078592:amyloid beta-protein (1-40); D010569:Perylene; C004965:hypericin