Amyloid fibril formation by bovine cytochrome c

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28 Citations (Scopus)

Abstract

Bovine heart cytochrome c is an all-α globular protein containing a covalently bound heme group. Prolonged incubation at 75°C in mild alkaline solution damages the prosthetic group and results in permanent unfolding of the polypeptide chain. Under this conditions, cytochrome c aggregates into fibrillar structures. Characterization by transmission electron microscopy and thioflavin-T binding assays shows that these species posses the characteristics of fibrils associated with the family of amyloid diseases. Our findings indicate that destabilization of the native fold of this highly α-helical protein can lead to its polymerization into β-sheet rich structures and suggest that this process does not depend on the population of partially folded monomeric states with extensive β-sheet structure. © 2005 - IOS Press and the authors. All rights reserved.
Original languageEnglish
Pages (from-to)199-205
JournalSpectroscopy
Volume19
Issue number4
DOIs
Publication statusPublished - 1 Jan 2005

Keywords

  • Amyloid formation
  • Cytochrome c
  • Helical proteins
  • Protein denaturation
  • Protein misfolding

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