0000000000666746
AUTHOR
S Mangialardo
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 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 re…
Aggregation properties of proteins under high pressure
Fourier transform infrared spectroscopy (FTIR) coupled with High Pressure (HP) techniques is a suitable tool to investigate unfolding/misfolding processes providing useful information on the kinetics of aggregation of proteins[1]. Since HP affects only the volume contribution to the Gibbs free energy, it is able to perturb the structure of proteins in a reversible way [2][3]. The principle governing pressure effects is that it tends to shift a system towards the state that occupies the smallest volume, it causes the electrostriction of charged and polar groups, the elimination of packing defects, and the solvation of hydrophobic groups. Cavities and packing defects are expected to be major …