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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and Woochun Chun

Volume 9, Issue 4, 2002

Page: [315 - 321] Pages: 7

DOI: 10.2174/0929866023408599

Price: $65

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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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