Predicted fold for the ABri amyloid subunit: A model for amyloidogenesis in Familial British Dementia

D. Mahadevan, T. Chattopadhyay, R. A. Palmer, R. O'Brien, J. W. Saldanha

Research output: Contribution to journalArticle

2 Scopus citations

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 β-strands forming an antiparallel β-sheet and a small C-terminal α-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 β-sheet structure with a small tx-helical component.

Original languageEnglish (US)
Pages (from-to)139-146
Number of pages8
JournalProtein and Peptide Letters
Volume8
Issue number2
DOIs
StatePublished - May 22 2001
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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