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

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.

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