Amyloid fibril formation by bovine cytochrome c. Issue 4 (2005)

• Record Type: Journal Article
• Authors: de Groot de Groot, Natalia S. Natalia S.; Ventura Ventura, Salvador Salvador
• Is Part Of: Spectroscopy. Volume 19:Issue 4(2005)
• Page Start: 199
• Page End: 205
• Publication Date: 2005
• Subjects: Amyloid formation -- cytochrome c -- protein misfolding -- protein denaturation -- helical proteins
• DOI: 10.1155/2005/104348
• Languages: English
• ISSNs: 0712-4813

Abstract

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.