Inhibiting effect of α(s1)-casein on Aβ(1-40) fibrillogenesis

α(s1)-Casein is one of the four types of caseins, the largest protein component of bovine milk. The lack of a compact folded conformation and the capability to form micelles suggest a relationship of α(s1)-casein with the class of the intrinsically disordered (or natively unfolded) proteins. These p...

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Vydané v:Biochimica et biophysica acta Ročník 1820; číslo 2; s. 124
Hlavní autori: Carrotta, R, Canale, C, Diaspro, A, Trapani, A, Biagio, P L San, Bulone, D
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Netherlands 01.02.2012
Predmet:
Amyloid - drug effects
Amyloid beta-Peptides - antagonists & inhibitors
Amyloid beta-Peptides - metabolism
Caseins - pharmacology
Circular Dichroism
Hydrodynamics
Light
Microscopy, Atomic Force
Particle Size
Peptide Fragments - antagonists & inhibitors
Peptide Fragments - metabolism
Protein Structure, Quaternary
Scattering, Radiation
Spectrometry, Fluorescence
Thiazoles - metabolism
Time Factors
ISSN:0006-3002
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Shrnutí:α(s1)-Casein is one of the four types of caseins, the largest protein component of bovine milk. The lack of a compact folded conformation and the capability to form micelles suggest a relationship of α(s1)-casein with the class of the intrinsically disordered (or natively unfolded) proteins. These proteins are known to exert a stabilizing activity on biomolecules through specific interaction with hydrophobic surfaces. In the present work we focused on the effect of α(s1)-casein on the fibrillogenesis of 1-40 β-amyloid peptide, involved in Alzheimer's disease. The aggregation kinetics of β-peptide in presence and absence of α(s1)-casein was followed under shear at 37°C by recording the Thioflavine fluorescence, usually taken as an indicator of fibers formation. Measurements of Static and Dynamic Light Scattering, Circular Dichroism, and AFM imaging were done to reveal the details of α(s1)-casein-Aβ(1-40) interaction. α(s1)-Casein addition sizably increases the lag-time of the nucleation phase and slows down the entire fibrillization process. α(s1)-Casein sequesters the amyloid peptide on its surface thus exerting a chaperone-like activity by means a colloidal inhibition mechanism. Insights on the working mechanism of natural chaperones in preventing or controlling the amyloid aggregation.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0006-3002
DOI:10.1016/j.bbagen.2011.11.010