Abstract
ABri is a 34 residue polypeptide that forms amyloid fibrils in Familial British Dementia (FBD). A PSI-Blast search, 3 different fold recognition programs and 3D model-building indicated that it has 3 beta-strands forming an antiparallel beta-sheet and a small C-terminal alpha-helix. In order to validate the prediction, the region coding the ABri polypeptide was cloned, expressed and purified from E.Coli. Circular Dichroism (CD) spectroscopy of ABri in aqueous solution shows it to have a predominantly beta-sheet structure with a small alpha-helical component.
Keywords: ABRI AMYLOID SUBUNIT, AMYLOIDOGENESIS, FAMILIAL BRITISH DEMENTIA, human homologue (BRi), ABri amyloid polypeptide
Protein & Peptide Letters
Title: Predicted fold for the ABri Amyloid Subunit: A Model for Amyloidogenesis in Familial British Dementia.
Volume: 8 Issue: 3
Author(s): Daruka Mahadevan, Tapan Chattopadhyay, Rex A. Palmer, Ronan O Brien and Jose W. Saldanha
Affiliation:
Keywords: ABRI AMYLOID SUBUNIT, AMYLOIDOGENESIS, FAMILIAL BRITISH DEMENTIA, human homologue (BRi), ABri amyloid polypeptide
Abstract: ABri is a 34 residue polypeptide that forms amyloid fibrils in Familial British Dementia (FBD). A PSI-Blast search, 3 different fold recognition programs and 3D model-building indicated that it has 3 beta-strands forming an antiparallel beta-sheet and a small C-terminal alpha-helix. In order to validate the prediction, the region coding the ABri polypeptide was cloned, expressed and purified from E.Coli. Circular Dichroism (CD) spectroscopy of ABri in aqueous solution shows it to have a predominantly beta-sheet structure with a small alpha-helical component.
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Cite this article as:
Mahadevan Daruka, Chattopadhyay Tapan, Palmer A. Rex, O Brien Ronan and Saldanha W. Jose, Predicted fold for the ABri Amyloid Subunit: A Model for Amyloidogenesis in Familial British Dementia., Protein & Peptide Letters 2001; 8 (3) . https://dx.doi.org/10.2174/0929866013409472
DOI https://dx.doi.org/10.2174/0929866013409472 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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