Raman analysis of insulin denaturation induced by high-pressure and thermal treatments
Version of Record online: 11 NOV 2011
Copyright © 2011 John Wiley & Sons, Ltd.
Journal of Raman Spectroscopy
Volume 43, Issue 6, pages 692–700, June 2012
How to Cite
Mangialardo, S., Piccirilli, F., Perucchi, A., Dore, P. and Postorino, P. (2012), Raman analysis of insulin denaturation induced by high-pressure and thermal treatments. J. Raman Spectrosc., 43: 692–700. doi: 10.1002/jrs.3097
- Issue online: 18 JUN 2012
- Version of Record online: 11 NOV 2011
- Manuscript Accepted: 30 SEP 2011
- Manuscript Revised: 28 SEP 2011
- Manuscript Received: 2 AUG 2011
- raman spectroscopy;
- high pressure;
- phase transition;
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. Copyright © 2011 John Wiley & Sons, Ltd.