Abstract
A colostral proline-rich polypeptide complex (PRP) consisting of over 30 peptides shows beneficial effects in Alzheimer's disease (AD) patients when administered in the form of sublinqual tablets called Colostrinin. The aim of the present studies was to investigate whether nanopeptide fragment of PRP (NP) - one of the PRP complex components can affect aggregation of amyloid beta (Abeta1-42). The effect of NP on Abeta aggregation was studied using Thioflavin T (ThT) binding, atomic force microscopy, and analyzing circular dichroism spectra. Results presented suggest that NP can directly interact with amyloid beta, inhibit its aggregation and disrupt existing aggregates acting as a beta sheet breaker and reduce toxicity induced by aggregated forms of Abeta.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / drug effects*
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Amyloid beta-Peptides / metabolism
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Animals
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Benzothiazoles
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Cell Line, Tumor
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Cell Survival / drug effects
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Circular Dichroism
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Fluorescent Dyes / chemistry
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Microscopy, Atomic Force
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Nanostructures*
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Oligopeptides / pharmacology*
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Peptide Fragments / chemistry
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Peptide Fragments / drug effects*
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Peptide Fragments / metabolism
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Protein Structure, Secondary / drug effects
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Rats
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Sheep, Domestic / metabolism*
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Thiazoles / chemistry
Substances
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Amyloid beta-Peptides
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Benzothiazoles
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Fluorescent Dyes
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Oligopeptides
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Peptide Fragments
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Thiazoles
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amyloid beta-protein (1-42)
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valyl-glutamyl-seryl-tyrosyl-valyl-prolyl-leucyl-phenylalanylproline
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thioflavin T