Abstract

A prion determining 7-mer peptide derived from Sup35 was fused to glutathione S transferase (GST). The fusion protein was successfully overexpressed in Escherichia coli, and purified by employing affinity chromatography.Upon incubation, it showed substantial aggregation suggesting the formation of amyloid-like fibrils. Congo Red binding strongly suggested that the fusion protein formed amyloid-like fibrils. By considering the steric hindrance of GST, the β-sheet formation should be in the anti-parallel fashion.

Keywords: Prionogenic Peptide, Amyloid, 7-mer peptide, glutathione S transferase, Escherichia coli, anti-parallel fashion