On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.

Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies. One of the characteristic features of amyloid fibrils is the high thermodynamic stability relative both to native and disordered states w...

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Autores principales:	Weronika Surmacz-Chwedoruk, Iwona Malka, Łukasz Bożycki, Hanna Nieznańska, Wojciech Dzwolak
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b31ee8b3fde1447ebeefd06a43bea34e
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spelling	oai:doaj.org-article:b31ee8b3fde1447ebeefd06a43bea34e2021-11-18T08:36:47ZOn the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.1932-620310.1371/journal.pone.0086320https://doaj.org/article/b31ee8b3fde1447ebeefd06a43bea34e2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24466022/?tool=EBIhttps://doaj.org/toc/1932-6203Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies. One of the characteristic features of amyloid fibrils is the high thermodynamic stability relative both to native and disordered states which is also thought to underlie the perplexingly remarkable heat resistance of prion infectivity. Here, we are comparing high-temperature degradation of native and fibrillar forms of human insulin. Decomposition of insulin amyloid has been studied under helium atmosphere and in the temperature range from ambient conditions to 750°C using thermogravimetry and differential scanning calorimetry coupled to mass spectrometry. While converting native insulin into amyloid does upshift onset of thermal decomposition by ca. 75°C, fibrils remain vulnerable to covalent degradation at temperatures below 300°C, as reflected by mass spectra of gases released upon heating of amyloid samples, as well as morphology and infrared spectra of fibrils subjected to incubation at 250°C. Mass spectra profiles of released gases indicate that degradation of fibrils is much more cooperative than degradation of native insulin. The data show no evidence of water of crystallization trapped within insulin fibrils. We have also compared untreated and heated amyloid samples in terms of capacity to seed daughter fibrils. Kinetic traces of seed-induced insulin fibrillation have shown that the seeding potency of amyloid samples decreases significantly already after exposure to 200°C, even though corresponding electron micrographs indicated persisting fibrillar morphology. Our results suggest that amyloid-based biological activity may not survive extremely high temperature treatments, at least in the absence of other stabilizing factors.Weronika Surmacz-ChwedorukIwona MalkaŁukasz BożyckiHanna NieznańskaWojciech DzwolakPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 1, p e86320 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Weronika Surmacz-Chwedoruk Iwona Malka Łukasz Bożycki Hanna Nieznańska Wojciech Dzwolak On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
description	Formation of amyloid fibrils in vivo has been linked to disorders such as Alzheimer's disease and prion-associated transmissible spongiform encephalopathies. One of the characteristic features of amyloid fibrils is the high thermodynamic stability relative both to native and disordered states which is also thought to underlie the perplexingly remarkable heat resistance of prion infectivity. Here, we are comparing high-temperature degradation of native and fibrillar forms of human insulin. Decomposition of insulin amyloid has been studied under helium atmosphere and in the temperature range from ambient conditions to 750°C using thermogravimetry and differential scanning calorimetry coupled to mass spectrometry. While converting native insulin into amyloid does upshift onset of thermal decomposition by ca. 75°C, fibrils remain vulnerable to covalent degradation at temperatures below 300°C, as reflected by mass spectra of gases released upon heating of amyloid samples, as well as morphology and infrared spectra of fibrils subjected to incubation at 250°C. Mass spectra profiles of released gases indicate that degradation of fibrils is much more cooperative than degradation of native insulin. The data show no evidence of water of crystallization trapped within insulin fibrils. We have also compared untreated and heated amyloid samples in terms of capacity to seed daughter fibrils. Kinetic traces of seed-induced insulin fibrillation have shown that the seeding potency of amyloid samples decreases significantly already after exposure to 200°C, even though corresponding electron micrographs indicated persisting fibrillar morphology. Our results suggest that amyloid-based biological activity may not survive extremely high temperature treatments, at least in the absence of other stabilizing factors.
format	article
author	Weronika Surmacz-Chwedoruk Iwona Malka Łukasz Bożycki Hanna Nieznańska Wojciech Dzwolak
author_facet	Weronika Surmacz-Chwedoruk Iwona Malka Łukasz Bożycki Hanna Nieznańska Wojciech Dzwolak
author_sort	Weronika Surmacz-Chwedoruk
title	On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
title_short	On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
title_full	On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
title_fullStr	On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
title_full_unstemmed	On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
title_sort	on the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/b31ee8b3fde1447ebeefd06a43bea34e
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On the heat stability of amyloid-based biological activity: insights from thermal degradation of insulin fibrils.

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