Raman spectroscopy has been used to investigate different conformational states of bovine pancreatic insulin: the native form and several structurally modified states with different extent of denaturation induced by thermo-chemical treatment and by applying very high pressure (up to 8 GPa) using a diamond anvil cell. High-pressure results confirm the peculiar strength to volume compression of insulin and largely extend the pressure range of its structural stability (0-4.2 GPa). Above 4.2 GPa, insulin undergoes an irreversible structural transition that, once pressure is released, leaves the sample in a new conformational state. The protein secondary structure after the pressure treatment results in a structure that is somewhat intermediate between that of the native and the thermo-chemical fibrillar samples. The analysis of the pressure dependence of the Raman spectrum and of several specific spectroscopic markers allows us to follow the path from the native to new pressure-denatured protein conformation.

Mangialardo, S., Piccirilli, F., Perucchi, A., Dore, P., Postorino, P. (2012). Raman analysis of insulin denaturation induced by high-pressure and thermal treatments. JOURNAL OF RAMAN SPECTROSCOPY, 43(6), 692-700 [10.1002/jrs.3097].

Raman analysis of insulin denaturation induced by high-pressure and thermal treatments

PICCIRILLI, Federica;
2012-01-01

Abstract

Raman spectroscopy has been used to investigate different conformational states of bovine pancreatic insulin: the native form and several structurally modified states with different extent of denaturation induced by thermo-chemical treatment and by applying very high pressure (up to 8 GPa) using a diamond anvil cell. High-pressure results confirm the peculiar strength to volume compression of insulin and largely extend the pressure range of its structural stability (0-4.2 GPa). Above 4.2 GPa, insulin undergoes an irreversible structural transition that, once pressure is released, leaves the sample in a new conformational state. The protein secondary structure after the pressure treatment results in a structure that is somewhat intermediate between that of the native and the thermo-chemical fibrillar samples. The analysis of the pressure dependence of the Raman spectrum and of several specific spectroscopic markers allows us to follow the path from the native to new pressure-denatured protein conformation.
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
Mangialardo, S., Piccirilli, F., Perucchi, A., Dore, P., Postorino, P. (2012). Raman analysis of insulin denaturation induced by high-pressure and thermal treatments. JOURNAL OF RAMAN SPECTROSCOPY, 43(6), 692-700 [10.1002/jrs.3097].
File in questo prodotto:
File Dimensione Formato  
Mangialardo_et_al-2012-Journal_of_Raman_Spectroscopy.pdf

Solo gestori archvio

Descrizione: pdf
Dimensione 301.83 kB
Formato Adobe PDF
301.83 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10447/65404
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 42
  • ???jsp.display-item.citation.isi??? 38
social impact