PUMA
Istituto di Biofisica     
Sgarbossa A., Buselli D., Lenci F. In vitro perturbation of aggregation processes in β-amyloid peptides: A spectroscopic study. In: 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., vol. 582 (23-24) pp. 3288 - 3292. Elsevier, 2008.
 
 
Abstract
(English)
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.
DOI: 10.1016/j.febslet.2008.08.039
Subject Alzheimer
β-Amyloid
Hypericin
Neurotoxic peptide
Intermolecular interaction


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