Bacterial Inclusion Bodies for Anti-Amyloid Drug Discovery: Current and Future Screening Methods.

Bacterial Inclusion Bodies for Anti-Amyloid Drug Discovery: Current and Future Screening Methods. Curr Protein Pept Sci. 2019 Mar 29;: Authors: Caballero AB, Espargarò A, Pont C, Busquets MA, Estelrich J, Muñoz-Torrero D, Gamez P, Sabate R Abstract Amyloid aggregation is linked to an increasing number of human disorders from non-neurological pathologies such as type-2 diabetes to neurodegenerative ones such as Alzheimer or Parkinson's diseases. Thirty-six human proteins have shown the capacity to aggregate into pathological amyloid structures. To date, it is widely accepted that amyloid folding/aggregation is a universal process present in eukaryotic and prokaryotic cells. In the last decade, several studies have unequivocally demonstrated that bacterial inclusion bodies - insoluble protein aggregates usually formed during heterologous protein overexpression in bacteria - are mainly composed of overexpressed proteins in amyloid conformation. This fact shows that amyloid-prone proteins display a similar aggregation propensity in humans and bacteria, opening the possibility to use bacteria as simple models to study amyloid aggregation process and the potential effect of both anti-amyloid drugs and pro-aggregative compounds. Under these considerations, several in vitro and in cellulo methods, which exploit the amyloid properties of bacterial inclusion bodies, have been proposed in the last few years. Since these new methods are fast, ...
Source: Current Protein and Peptide Science - Category: Biochemistry Authors: Tags: Curr Protein Pept Sci Source Type: research