Predicted Fold for the Abri Amyloid Subunit: A Model for Amyloidogenesis in Familial British Dementia

Authors: Mahadevan D.; Chattopadhyay T.; Palmer R.A.; O Brien R.; Saldanha J.W.

Source: Protein and Peptide Letters, Volume 8, Number 2, April 2001 , pp. 139-146(8)

Publisher: Bentham Science Publishers

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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: Amyloidogenesis

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409634

Publication date: 2001-04-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.