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  • Title: β-sheet interfering molecules acting against β-amyloid aggregation and fibrillogenesis.
    Author: Francioso A, Punzi P, Boffi A, Lori C, Martire S, Giordano C, D'Erme M, Mosca L.
    Journal: Bioorg Med Chem; 2015 Apr 15; 23(8):1671-83. PubMed ID: 25769517.
    Abstract:
    β-Sheet aggregates and amyloid fibrils rising from conformational changes of proteins are observed in several pathological human conditions. These structures are organized in β-strands that can reciprocally interact by hydrophobic and π-π interactions. The amyloid aggregates can give rise to pathological conditions through complex biochemical mechanisms whose physico-chemical nature has been understood in recent times. This review focuses on the various classes of natural and synthetic small molecules able to act against β-amyloid fibrillogenesis and toxicity that may represent new pharmacological tools in Alzheimer's diseases. Some peptides, named 'β-sheet breaker peptides', are able to hamper amyloid aggregation and fibrillogenesis by interfering with and destabilizing the non native β-sheet structures. Other natural compounds, like polyphenols or indolic molecules such as melatonin, can interfere with β-amyloid peptide pathogenicity by inhibiting aggregation and counteracting oxidative stress that is a key hallmark in Alzheimer's disease.
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