Anno2012
AutoriSantangelo MG; Noto R; Levantino M; Cupane A; Ricagno S, Pezzullo M, Bolognesi M, Mangione MR, Martorana V, Manno M
AbstractThe polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85°C, display the same isosbestic points in the Amide I2 band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45°C suggesting that the polymerization rate-limiting step is the formation of an activated monomeric species. The polymer structures are consistent with a model that predicts the bare insertion of portions of the reactive center loop into the A ²-sheet of neighboring serpin molecule, although with different extents at 45 and 85°C
RivistaProteins
ISSN0887-3585
Impact factor
Volume80
Pagina inizio13
Pagina fine8
Autori IBFMauro MANNO, Vincenzo MARTORANA, Rosina NOTO, Maria Rosalia MANGIONE, Martino BOLOGNESI, Margherita PEZZULLO
Linee di Ricerca IBFMD.P01.002.001, MD.P01.005.001
Sedi IBFIBF.MI, IBF.PA