On the molecular structure of human neuroserpin polymers

Maria Grazia Santangelo, Antonio Cupane, Matteo Levantino, Mauro Manno, Martino Bolognesi, Margherita Pezzullo, Stefano Ricagno, Maria Rosalia Mangione, Vincenzo Martorana, Rosina Noto

Risultato della ricerca: Articlepeer review

10 Citazioni (Scopus)

Abstract

The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. Here, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. Firstly we show that two distinct neuroserpin polymers, formed at 45 and 85 °C, display the same isosbestic points in the Amide I′ 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 monomericspecies. The polymer structures are consistent with a model that predicts the bare insertion of portions of the reactive center loop into the A β-sheet of neighboring serpin molecule, although with different extents at 45 and 85 °C.
Lingua originaleEnglish
pagine (da-a)8-13
Numero di pagine6
RivistaPROTEINS
Volume80
Stato di pubblicazionePublished - 2012

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1300.1303???
  • ???subjectarea.asjc.1300.1312???

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