Journal
PROTEIN AND PEPTIDE LETTERS
Volume 9, Issue 4, Pages 315-321Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929866023408599
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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.
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