Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Solution conditions can promote formation of either amyloid protofilamentsor mature fibrils from the HypF N-terminal domain
Autore:
Chiti, F; Bucciantini, M; Capanni, C; Taddei, N; Dobson, CM; Stefani, M;
Indirizzi:
Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England Univ Cambridge Cambridge England CB2 1EW hem, Cambridge CB2 1EW, England Univ Florence, Dipartimento Sci Biochim, I-50134 Florence, Italy Univ Florence Florence Italy I-50134 ci Biochim, I-50134 Florence, Italy
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 12, volume: 10, anno: 2001,
pagine: 2541 - 2547
SICI:
0961-8368(200112)10:12<2541:SCCPFO>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
IN-VITRO; PEPTIDE FRAGMENT; PROTEINS; TRANSTHYRETIN; LYSOZYME;
Keywords:
aggregation; amyloid fibrils; HypF N-terminal domain; protofilaments; trifluoroethanol;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Dobson, CM Univ Cambridge, Dept Chem, Lensfield Rd, Cambridge CB2 1EW, England Univ Cambridge Lensfield Rd Cambridge England CB2 1EW England
Citazione:
F. Chiti et al., "Solution conditions can promote formation of either amyloid protofilamentsor mature fibrils from the HypF N-terminal domain", PROTEIN SCI, 10(12), 2001, pp. 2541-2547

Abstract

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 trifluoro ethanol 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 23:33:22