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

Author(s): Young Kee Chae, Kyoung Suk Cho, Woochun Chun

Journal Name: Protein & Peptide Letters

Volume 9 , Issue 4 , 2002


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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 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

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Article Details

VOLUME: 9
ISSUE: 4
Year: 2002
Page: [315 - 321]
Pages: 7
DOI: 10.2174/0929866023408599
Price: $65

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