Amyloid fibril formation by bovine cytochrome c

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(Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura, Salvador

(Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)

Data:	2005
Resum:	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.
Nota:	Ajuts: S.V. is supported by a "Ramón y Cajal" project awarded by the MCYT and co-financed by the Universitat Autonoma de Barcelona.
Drets:	Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.
Llengua:	Anglès
Document:	Article ; recerca ; Versió publicada
Matèria:	Amyloid formation ; Cytochrome c ; Protein misfolding ; Protein denaturation ; Helical proteins
Publicat a:	Spectroscopy, Vol. 19 (2005) , p. 199-205, ISSN 0712-4813

8 p, 1.3 MB

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