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
Protein & Peptide Letters
Title: A Prionogenic Peptide Derived from Sup35 can Force the Whole Gst Fusion Protein to Show Amyloid Characteristics
Volume: 9 Issue: 4
Author(s): Young Kee Chae, Kyoung Suk Cho and Woochun Chun
Affiliation:
Keywords: Prionogenic Peptide, Amyloid, 7-mer peptide, glutathione S transferase, Escherichia coli, anti-parallel fashion
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.
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Cite this article as:
Chae Kee Young, Cho Suk Kyoung and Chun Woochun, A Prionogenic Peptide Derived from Sup35 can Force the Whole Gst Fusion Protein to Show Amyloid Characteristics, Protein & Peptide Letters 2002; 9 (4) . https://dx.doi.org/10.2174/0929866023408599
DOI https://dx.doi.org/10.2174/0929866023408599 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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