In vitro perturbation of aggregation processes in β‐amyloid peptides: A spectroscopic study

Autori: Sgarbossa, A., Buselli, D., and Lenci, F.
Rivista: FEBS Letters
DOI: 10.1016/j.febslet.2008.08.039
We have performed an in vitro study to investigate the molecular basis of the aggregation kinetic of 1-40 β-amyloid peptides (Aβ 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, α-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 Aβ peptides.

Keywords: Alzheimer, β-Amyloid, Hypericin, Neurotoxic peptide, Intermolecular interaction

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