Sequential dissociation of insulin amyloids probed by High Pressure Fourier Transform Infrared Spectroscopy

Federica Piccirilli, Andrea Perucchi, Paolo Postorino, Sara Mangialardo, Stefano Lupi, Federica Piccirilli, Leonetta Baldassarre

Research output: Contribution to journalArticle

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Abstract

High Pressure (HP) Fourier Transform Infrared Spectroscopy (FTIR) has been here employed to investigate the thermodynamic stability of bovine pancreatic insulin (BPI) amyloids. Once the aggregation reaction has started, the backbone arrangement of the proteins forming the amyloid is known to reach a stationary phase in few hours; after this time the infrared absorption of fibrils becomes stable. It is here shown how the further stabilization of the structure during the stationary phase can be probed via FTIR spectroscopy, through the observation of the high pressure behaviour of fibrils formed at different maturation stages. We report on the high pressure fragmentation of insulin amyloids, probed on fibrils formed in the early stages of the stationary phase. Moreover, we noticed a sequentiality in high pressure dissociation, that seems to respect a pre-existing hierarchy of structures: the stabilization of a protofibrillar state is observed at pressures in the order of few kbar and our results suggest the possible occurrence of a partial refolding, induced by pressures up to 11.4 kbar. Our findings remark the importance of high pressure in stabilizing intermediate structures and in evaluating the driving forces of fibrillation, demonstrating how the control of electrostatic interactions and hydrophobic effect can be used to characterize the factors that modulate amyloids stability.
Original languageEnglish
Pages (from-to)-
Number of pages9
JournalSoft Matter
VolumeXXX
Publication statusPublished - 2012

Fingerprint

insulin
Amyloid
Infrared spectroscopy
infrared spectroscopy
Mathematical transformations
dissociation
Insulin
stabilization
fibrillation
Stabilization
infrared absorption
hierarchies
fragmentation
Infrared absorption
Coulomb interactions
occurrences
electrostatics
proteins
thermodynamics
Thermodynamic stability

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Condensed Matter Physics

Cite this

Piccirilli, F., Perucchi, A., Postorino, P., Mangialardo, S., Lupi, S., Piccirilli, F., & Baldassarre, L. (2012). Sequential dissociation of insulin amyloids probed by High Pressure Fourier Transform Infrared Spectroscopy. Soft Matter, XXX, -.

Sequential dissociation of insulin amyloids probed by High Pressure Fourier Transform Infrared Spectroscopy. / Piccirilli, Federica; Perucchi, Andrea; Postorino, Paolo; Mangialardo, Sara; Lupi, Stefano; Piccirilli, Federica; Baldassarre, Leonetta.

In: Soft Matter, Vol. XXX, 2012, p. -.

Research output: Contribution to journalArticle

Piccirilli, F, Perucchi, A, Postorino, P, Mangialardo, S, Lupi, S, Piccirilli, F & Baldassarre, L 2012, 'Sequential dissociation of insulin amyloids probed by High Pressure Fourier Transform Infrared Spectroscopy', Soft Matter, vol. XXX, pp. -.
Piccirilli, Federica ; Perucchi, Andrea ; Postorino, Paolo ; Mangialardo, Sara ; Lupi, Stefano ; Piccirilli, Federica ; Baldassarre, Leonetta. / Sequential dissociation of insulin amyloids probed by High Pressure Fourier Transform Infrared Spectroscopy. In: Soft Matter. 2012 ; Vol. XXX. pp. -.
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AU - Piccirilli, Federica

AU - Perucchi, Andrea

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AU - Lupi, Stefano

AU - Piccirilli, Federica

AU - Baldassarre, Leonetta

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N2 - High Pressure (HP) Fourier Transform Infrared Spectroscopy (FTIR) has been here employed to investigate the thermodynamic stability of bovine pancreatic insulin (BPI) amyloids. Once the aggregation reaction has started, the backbone arrangement of the proteins forming the amyloid is known to reach a stationary phase in few hours; after this time the infrared absorption of fibrils becomes stable. It is here shown how the further stabilization of the structure during the stationary phase can be probed via FTIR spectroscopy, through the observation of the high pressure behaviour of fibrils formed at different maturation stages. We report on the high pressure fragmentation of insulin amyloids, probed on fibrils formed in the early stages of the stationary phase. Moreover, we noticed a sequentiality in high pressure dissociation, that seems to respect a pre-existing hierarchy of structures: the stabilization of a protofibrillar state is observed at pressures in the order of few kbar and our results suggest the possible occurrence of a partial refolding, induced by pressures up to 11.4 kbar. Our findings remark the importance of high pressure in stabilizing intermediate structures and in evaluating the driving forces of fibrillation, demonstrating how the control of electrostatic interactions and hydrophobic effect can be used to characterize the factors that modulate amyloids stability.

AB - High Pressure (HP) Fourier Transform Infrared Spectroscopy (FTIR) has been here employed to investigate the thermodynamic stability of bovine pancreatic insulin (BPI) amyloids. Once the aggregation reaction has started, the backbone arrangement of the proteins forming the amyloid is known to reach a stationary phase in few hours; after this time the infrared absorption of fibrils becomes stable. It is here shown how the further stabilization of the structure during the stationary phase can be probed via FTIR spectroscopy, through the observation of the high pressure behaviour of fibrils formed at different maturation stages. We report on the high pressure fragmentation of insulin amyloids, probed on fibrils formed in the early stages of the stationary phase. Moreover, we noticed a sequentiality in high pressure dissociation, that seems to respect a pre-existing hierarchy of structures: the stabilization of a protofibrillar state is observed at pressures in the order of few kbar and our results suggest the possible occurrence of a partial refolding, induced by pressures up to 11.4 kbar. Our findings remark the importance of high pressure in stabilizing intermediate structures and in evaluating the driving forces of fibrillation, demonstrating how the control of electrostatic interactions and hydrophobic effect can be used to characterize the factors that modulate amyloids stability.

KW - high pressure; amyloids; insulin; FTIR

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