Sequential dissociation of insulin amyloids probed by High PressureFourier Transform Infrared Spectroscopy

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

Risultato della ricerca: Article

12 Citazioni (Scopus)

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 ofthe 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 probedvia 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.
Lingua originaleEnglish
Numero di pagine9
RivistaDefault journal
VolumeXXX
Stato di pubblicazionePublished - 2012

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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

Cita questo

Piccirilli, F., Mangialardo, S., Lupi, S., Piccirilli, F., Baldassarre, L., Perucchi, A., & Postorino, P. (2012). Sequential dissociation of insulin amyloids probed by High PressureFourier Transform Infrared Spectroscopy. Default journal, XXX.

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

In: Default journal, Vol. XXX, 2012.

Risultato della ricerca: Article

Piccirilli, F, Mangialardo, S, Lupi, S, Piccirilli, F, Baldassarre, L, Perucchi, A & Postorino, P 2012, 'Sequential dissociation of insulin amyloids probed by High PressureFourier Transform Infrared Spectroscopy', Default journal, vol. XXX.
Piccirilli, Federica ; Mangialardo, Sara ; Lupi, Stefano ; Piccirilli, Federica ; Baldassarre, Leonetta ; Perucchi, Andrea ; Postorino, Paolo. / Sequential dissociation of insulin amyloids probed by High PressureFourier Transform Infrared Spectroscopy. In: Default journal. 2012 ; Vol. XXX.
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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 ofthe 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 probedvia 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.",
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T1 - Sequential dissociation of insulin amyloids probed by High PressureFourier Transform Infrared Spectroscopy

AU - Piccirilli, Federica

AU - Mangialardo, Sara

AU - Lupi, Stefano

AU - Piccirilli, Federica

AU - Baldassarre, Leonetta

AU - Perucchi, Andrea

AU - Postorino, Paolo

PY - 2012

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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 ofthe 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 probedvia 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 ofthe 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 probedvia 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.

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KW - amyloids

KW - high pressure

KW - insulin

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