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1 Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy
2 Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom
Reprint requests to: Christopher M. Dobson, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK; e-mail: cmd44{at}cam.ac.uk; fax: 44-1223-763418 or Massimo Stefani, Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, 50134 Firenze, Italy; e-mail: stefani{at}scibio.unifi.it; fax: 39-055-4222725.
The HypF N-terminal domain has been found to convert readily from its native globular conformation into protein aggregates with the characteristics of amyloid fibrils associated with a variety of human diseases. This conversion was achieved by incubation at acidic pH or in the presence of moderate concentrations of trifluoroethanol. Electron microscopy showed that the fibrils grown in the presence of trifluoroethanol were predominantly 3–5 nm and 7–9 nm in width, whereas fibrils of 7–9 nm and 12–20 nm in width prevailed in samples incubated at acidic pH. These results indicate that the assembly of protofilaments or narrow fibrils into mature amyloid fibrils is guided by interactions between hydrophobic residues that may remain exposed on the surface of individual protofilaments. Therefore, formation and isolation of individual protofilaments appears facilitated under conditions that favor the destabilization of hydrophobic interactions, such as in the presence of trifluoroethanol.
Keywords: Aggregation; amyloid fibrils; HypF N-terminal domain; protofilaments; trifluoroethanol
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