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A Prionogenic Peptide Derived from Sup35 can Force the Whole Gst Fusion Protein to Show Amyloid Characteristics

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

Document Type: Review Article


Publication date: August 1, 2002

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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