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The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

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The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. / van Gils, Juami Hermine Mariama; van Dijk, Erik; Peduzzo, Alessia; Hofmann, Alexander; Vettore, Nicola; Schützmann, Marie P; Groth, Georg; Mouhib, Halima; Otzen, Daniel E; Buell, Alexander K; Abeln, Sanne.

I: PLOS Computational Biology, Bind 16, Nr. 5, e1007767, 05.2020.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

van Gils, JHM, van Dijk, E, Peduzzo, A, Hofmann, A, Vettore, N, Schützmann, MP, Groth, G, Mouhib, H, Otzen, DE, Buell, AK & Abeln, S 2020, 'The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth', PLOS Computational Biology, bind 16, nr. 5, e1007767. https://doi.org/10.1371/journal.pcbi.1007767

APA

van Gils, J. H. M., van Dijk, E., Peduzzo, A., Hofmann, A., Vettore, N., Schützmann, M. P., Groth, G., Mouhib, H., Otzen, D. E., Buell, A. K., & Abeln, S. (2020). The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLOS Computational Biology, 16(5), [e1007767]. https://doi.org/10.1371/journal.pcbi.1007767

CBE

van Gils JHM, van Dijk E, Peduzzo A, Hofmann A, Vettore N, Schützmann MP, Groth G, Mouhib H, Otzen DE, Buell AK, Abeln S. 2020. The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLOS Computational Biology. 16(5):Article e1007767. https://doi.org/10.1371/journal.pcbi.1007767

MLA

Vancouver

van Gils JHM, van Dijk E, Peduzzo A, Hofmann A, Vettore N, Schützmann MP o.a. The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. PLOS Computational Biology. 2020 maj;16(5). e1007767. https://doi.org/10.1371/journal.pcbi.1007767

Author

van Gils, Juami Hermine Mariama ; van Dijk, Erik ; Peduzzo, Alessia ; Hofmann, Alexander ; Vettore, Nicola ; Schützmann, Marie P ; Groth, Georg ; Mouhib, Halima ; Otzen, Daniel E ; Buell, Alexander K ; Abeln, Sanne. / The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth. I: PLOS Computational Biology. 2020 ; Bind 16, Nr. 5.

Bibtex

@article{8799955b8d2a4cb488d59604677d412d,
title = "The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth",
abstract = "Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer's and Parkinson's disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using a combination of theory, in vitro experiments, simulations of a coarse-grained protein model and meta-data analysis, we delineate the enthalpic and entropic contributions that dominate amyloid fibril elongation. Our prediction of a characteristic temperature-dependent enthalpic signature is confirmed by the performed calorimetric experiments and a meta-analysis over published data. From these results we are able to define the necessary conditions to observe cold denaturation of amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.",
author = "{van Gils}, {Juami Hermine Mariama} and {van Dijk}, Erik and Alessia Peduzzo and Alexander Hofmann and Nicola Vettore and Sch{\"u}tzmann, {Marie P} and Georg Groth and Halima Mouhib and Otzen, {Daniel E} and Buell, {Alexander K} and Sanne Abeln",
year = "2020",
month = may,
doi = "10.1371/journal.pcbi.1007767",
language = "English",
volume = "16",
journal = "P L o S Computational Biology (Online)",
issn = "1553-7358",
publisher = "public library of science",
number = "5",

}

RIS

TY - JOUR

T1 - The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

AU - van Gils, Juami Hermine Mariama

AU - van Dijk, Erik

AU - Peduzzo, Alessia

AU - Hofmann, Alexander

AU - Vettore, Nicola

AU - Schützmann, Marie P

AU - Groth, Georg

AU - Mouhib, Halima

AU - Otzen, Daniel E

AU - Buell, Alexander K

AU - Abeln, Sanne

PY - 2020/5

Y1 - 2020/5

N2 - Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer's and Parkinson's disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using a combination of theory, in vitro experiments, simulations of a coarse-grained protein model and meta-data analysis, we delineate the enthalpic and entropic contributions that dominate amyloid fibril elongation. Our prediction of a characteristic temperature-dependent enthalpic signature is confirmed by the performed calorimetric experiments and a meta-analysis over published data. From these results we are able to define the necessary conditions to observe cold denaturation of amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.

AB - Many proteins have the potential to aggregate into amyloid fibrils, protein polymers associated with a wide range of human disorders such as Alzheimer's and Parkinson's disease. The thermodynamic stability of amyloid fibrils, in contrast to that of folded proteins, is not well understood: the balance between entropic and enthalpic terms, including the chain entropy and the hydrophobic effect, are poorly characterised. Using a combination of theory, in vitro experiments, simulations of a coarse-grained protein model and meta-data analysis, we delineate the enthalpic and entropic contributions that dominate amyloid fibril elongation. Our prediction of a characteristic temperature-dependent enthalpic signature is confirmed by the performed calorimetric experiments and a meta-analysis over published data. From these results we are able to define the necessary conditions to observe cold denaturation of amyloid fibrils. Overall, we show that amyloid fibril elongation is associated with a negative heat capacity, the magnitude of which correlates closely with the hydrophobic surface area that is buried upon fibril formation, highlighting the importance of hydrophobicity for fibril stability.

U2 - 10.1371/journal.pcbi.1007767

DO - 10.1371/journal.pcbi.1007767

M3 - Journal article

C2 - 32365068

VL - 16

JO - P L o S Computational Biology (Online)

JF - P L o S Computational Biology (Online)

SN - 1553-7358

IS - 5

M1 - e1007767

ER -