Reference: Chae YK, et al. (2002) A prionogenic peptide derived from Sup35 can force the whole GST fusion protein to show amyloid characteristics. Protein Pept Lett 9(4):315-21

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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 beta-sheet formation should be in the anti-parallel fashion.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Chae YK, Cho KS, Chun W
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