Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential(127 visite) Di Gaetano S, Guglielmi F, Arciello A, Mangione P, Monti M, Pagnozzi D, Raimondi S, Giorgetti S, Orru S, Canale C, Pucci P, Dobson CM, Bellotti V, Piccoli R
Biochemical And Biophysical Research Communications (ISSN: 0006-291x, 0006-291xprint), 2006 Dec 8; 351(1): 223-228.
Tipo di articolo: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.855, Impact factor a 5 anni: 2.474
*** IBB - CNR *** Istituto di Biostrutture e Bioimmagini, CNR, Napoli, 80134, Italy Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, via Cinthia 4, Napoli, 80126, Italy Dipartimento di Biochimica, Università di Pavia, Pavia, 27100, Italy CEINGE Biotecnologie Avanzate, Napoli, 80131, Italy Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Napoli, 80126, Italy Laboratorio di Biotecnologie IRCCS, Pavia, 27100, Italy Dipartimento di Fisica, Università di Genova, Genova, 16146, Italy Department of Chemistry, University of Cambridge, Cambridge, CB2 IEW, United Kingdom
Riferimenti:
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Rogers, D. P., Brouillette, C. G., Engler, J. A., Tendian, S. W., Roberts, L., Mishra, V. K., Anantharamaiah, G. M., Ray, M. J., Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation (1997) Biochemistry, 36, pp. 288-300
Semisotnov, G. V., Rodinova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., Gilmanshin, R. I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
A variety of amyloid diseases are associated with fibrillar aggregates from N-terminal fragments of ApoA-I generated through a largely unexplored multi-step process. The understanding of the molecular mechanism is impaired by the lack of suitable amounts of the fibrillogenic polypeptides that could not be produced by recombinant methods so far. We report the production and the conformational analysis of recombinant ApoA-I 1-93 fragment. Similarly to the polypeptide isolated ex vivo, a pH switch from 7 to 4 induces a fast and reversible conformational transition to a helical state and leads to the identification of a key intermediate in the fibrillogenesis process. Limited proteolysis experiments suggested that the C-terminal region is involved in helix formation. The recombinant polypeptide generates fibrils at pH 4 on a time scale comparable with that of the native fragment. These findings open the way to studies on structural, thermodynamic, and kinetic aspects of ApoA-I fibrillogenesis. (c) 2006 Elsevier Inc. All rights reserved.
138 Records (138 escludendo Abstract e Conferenze). Impact factor totale: 539.935 (539.935 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 554.093 (554.093 escludendo Abstract e Conferenze).
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