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

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 d...

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Bibliographic Details
Published in:Journal of Raman spectroscopy 2012-06, Vol.43 (6), p.692-700
Main Authors: Mangialardo, S., Piccirilli, F., Perucchi, A., Dore, P., Postorino, P.
Format: Article
Language:English
Subjects:
Compressive strength
Denaturation
Diamond anvil cells
high pressure
Insulin
phase transition
protein
Proteins
Raman spectroscopy
Strength
Structural stability
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Summary: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. Raman spectroscopy has been used to investigate different conformational states of 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. Above 4.2 Gpa, insulin undergoes an irreversible transition to a new conformational state.
ISSN:0377-0486
1097-4555
DOI:10.1002/jrs.3097