Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin

Research output: Contribution to journal › Journal article › Research › peer-review

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Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin. / Bucciarelli, Saskia; Sayedi, Edres Sayed; Osella, Silvio; Trzaskowski, Bartosz; Vissing, Karina Juul; Vestergaard, Bente; Foderà, Vito.

In: Journal of Colloid and Interface Science, Vol. 561, 2020, p. 749-761.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Bucciarelli, S, Sayedi, ES, Osella, S, Trzaskowski, B, Vissing, KJ, Vestergaard, B & Foderà, V 2020, 'Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin', Journal of Colloid and Interface Science, vol. 561, pp. 749-761. https://doi.org/10.1016/j.jcis.2019.11.051

APA

Bucciarelli, S., Sayedi, E. S., Osella, S., Trzaskowski, B., Vissing, K. J., Vestergaard, B., & Foderà, V. (2020). Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin. Journal of Colloid and Interface Science, 561, 749-761. https://doi.org/10.1016/j.jcis.2019.11.051

Vancouver

Bucciarelli S, Sayedi ES, Osella S, Trzaskowski B, Vissing KJ, Vestergaard B et al. Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin. Journal of Colloid and Interface Science. 2020;561:749-761. https://doi.org/10.1016/j.jcis.2019.11.051

Author

Bucciarelli, Saskia ; Sayedi, Edres Sayed ; Osella, Silvio ; Trzaskowski, Bartosz ; Vissing, Karina Juul ; Vestergaard, Bente ; Foderà, Vito. / Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin. In: Journal of Colloid and Interface Science. 2020 ; Vol. 561. pp. 749-761.

Bibtex

@article{eb20598b0c7c4c0db99345e6ad476739,
title = "Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin",
abstract = "Protein (mis)folding, stability and aggregation are of interest in numerous fields, such as food sciences, biotechnology, and health sciences, and efforts are directed towards the elucidation of the underlying molecular mechanisms. Through an integrative approach, we show that a subtle balance between hydrogen bond formation and hydrophobic interactions defines protein self-assembly pathways. Hydrophobic co-solvents, such as monohydric alcohols, modulate these two forces through a combination of direct solvent-protein and solvent-mediated interactions, depending on the size of the alcohol. This affects the initial conformation of the model protein α-lactalbumin, which can be linked to variations of its fibrillation propensity, as well as the morphology of the final structures. These findings pave the way towards a better understanding of the forces governing protein self-assembly, allowing the development of strategies to suppress unwanted aggregation and control the growth of tuneable protein-based biomaterials.",
keywords = "Alcohols, Amyloid aggregation, Molecular dynamics, Protein hydration, Protein-protein Interactions, Smallangle X-ray scattering",
author = "Saskia Bucciarelli and Sayedi, {Edres Sayed} and Silvio Osella and Bartosz Trzaskowski and Vissing, {Karina Juul} and Bente Vestergaard and Vito Foder{\`a}",
year = "2020",
doi = "10.1016/j.jcis.2019.11.051",
language = "English",
volume = "561",
pages = "749--761",
journal = "Journal of Colloid and Interface Science",
issn = "0021-9797",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - Disentangling the role of solvent polarity and protein solvation in folding and self-assembly of α-lactalbumin

AU - Bucciarelli, Saskia

AU - Sayedi, Edres Sayed

AU - Osella, Silvio

AU - Trzaskowski, Bartosz

AU - Vissing, Karina Juul

AU - Vestergaard, Bente

AU - Foderà, Vito

PY - 2020

Y1 - 2020

N2 - Protein (mis)folding, stability and aggregation are of interest in numerous fields, such as food sciences, biotechnology, and health sciences, and efforts are directed towards the elucidation of the underlying molecular mechanisms. Through an integrative approach, we show that a subtle balance between hydrogen bond formation and hydrophobic interactions defines protein self-assembly pathways. Hydrophobic co-solvents, such as monohydric alcohols, modulate these two forces through a combination of direct solvent-protein and solvent-mediated interactions, depending on the size of the alcohol. This affects the initial conformation of the model protein α-lactalbumin, which can be linked to variations of its fibrillation propensity, as well as the morphology of the final structures. These findings pave the way towards a better understanding of the forces governing protein self-assembly, allowing the development of strategies to suppress unwanted aggregation and control the growth of tuneable protein-based biomaterials.

AB - Protein (mis)folding, stability and aggregation are of interest in numerous fields, such as food sciences, biotechnology, and health sciences, and efforts are directed towards the elucidation of the underlying molecular mechanisms. Through an integrative approach, we show that a subtle balance between hydrogen bond formation and hydrophobic interactions defines protein self-assembly pathways. Hydrophobic co-solvents, such as monohydric alcohols, modulate these two forces through a combination of direct solvent-protein and solvent-mediated interactions, depending on the size of the alcohol. This affects the initial conformation of the model protein α-lactalbumin, which can be linked to variations of its fibrillation propensity, as well as the morphology of the final structures. These findings pave the way towards a better understanding of the forces governing protein self-assembly, allowing the development of strategies to suppress unwanted aggregation and control the growth of tuneable protein-based biomaterials.

KW - Alcohols

KW - Amyloid aggregation

KW - Molecular dynamics

KW - Protein hydration

KW - Protein-protein Interactions

KW - Smallangle X-ray scattering

U2 - 10.1016/j.jcis.2019.11.051

DO - 10.1016/j.jcis.2019.11.051

M3 - Journal article

C2 - 31771874

AN - SCOPUS:85075978776

VL - 561

SP - 749

EP - 761

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

ER -

ID: 248568292