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Updated: Aug 19, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
Published on: December 19, 2015
Characterization of presenilin-amyloid precursor interaction using bacterial expression and two-hybrid systems for
Mona Harnasch1, Sandra Grau, Christian Behrends
1Cardiff School of Biosciences, Cardiff University, Cardiff CF10 3US, UK.
Abstract:
An Escherichia coli system was used to produce the human membrane proteins presenilin 1 and amyloid precursor protein and to analyse their interaction. Our data indicate that the main binding site for amyloid precursor protein is located in the N-terminal three-transmembrane segments of presenilin and not in the proposed active site containing the two conserved aspartate residues. The data also suggest the presence of an additional segment of sufficient hydrophobicity at the C-terminus of PS1 to act potentially as a transmembrane segment. The implications of these findings for the function of gamma-secretase are discussed.
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