Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach

Felix Roosen-Runge; Alessandro Gulotta; Saskia Bucciarelli; Lucía Casal-Dujat; Tommy Garting; Nicholas Skar-Gislinge; Marc Obiols-Rabasa; Bela Farago; Emanuela Zaccarelli; Peter Schurtenberger; Anna Stradner

doi:10.1016/j.bpj.2020.10.035

Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach

Felix Roosen-Runge^*, Alessandro Gulotta, Saskia Bucciarelli, Lucía Casal-Dujat, Tommy Garting, Nicholas Skar-Gislinge, Marc Obiols-Rabasa, Bela Farago, Emanuela Zaccarelli, Peter Schurtenberger, Anna Stradner

^*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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Abstract

We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.

Originalsprog	Engelsk
Tidsskrift	Biophysical Journal
Vol/bind	119
Udgave nummer	12
Sider (fra-til)	2483-2496
Antal sider	14
ISSN	0006-3495
DOI	https://doi.org/10.1016/j.bpj.2020.10.035
Status	Udgivet - 15 dec. 2020
Udgivet eksternt	Ja

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Roosen-Runge, F., Gulotta, A., Bucciarelli, S., Casal-Dujat, L., Garting, T., Skar-Gislinge, N., Obiols-Rabasa, M., Farago, B., Zaccarelli, E., Schurtenberger, P., & Stradner, A. (2020). Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach. Biophysical Journal, 119(12), 2483-2496. https://doi.org/10.1016/j.bpj.2020.10.035

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title = "Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach",

abstract = "We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.",

author = "Felix Roosen-Runge and Alessandro Gulotta and Saskia Bucciarelli and Luc{\'i}a Casal-Dujat and Tommy Garting and Nicholas Skar-Gislinge and Marc Obiols-Rabasa and Bela Farago and Emanuela Zaccarelli and Peter Schurtenberger and Anna Stradner",

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Roosen-Runge, F, Gulotta, A, Bucciarelli, S, Casal-Dujat, L, Garting, T, Skar-Gislinge, N, Obiols-Rabasa, M, Farago, B, Zaccarelli, E, Schurtenberger, P & Stradner, A 2020, 'Crowding in the Eye Lens: Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach', Biophysical Journal, bind 119, nr. 12, s. 2483-2496. https://doi.org/10.1016/j.bpj.2020.10.035

TY - JOUR

T1 - Crowding in the Eye Lens

T2 - Modeling the Multisubunit Protein β-Crystallin with a Colloidal Approach

AU - Roosen-Runge, Felix

AU - Gulotta, Alessandro

AU - Bucciarelli, Saskia

AU - Casal-Dujat, Lucía

AU - Garting, Tommy

AU - Skar-Gislinge, Nicholas

AU - Obiols-Rabasa, Marc

AU - Farago, Bela

AU - Zaccarelli, Emanuela

AU - Schurtenberger, Peter

AU - Stradner, Anna

PY - 2020/12/15

Y1 - 2020/12/15

N2 - We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.

AB - We present a multiscale characterization of aqueous solutions of the bovine eye lens protein βH crystallin from dilute conditions up to dynamical arrest, combining dynamic light scattering, small-angle x-ray scattering, tracer-based microrheology, and neutron spin echo spectroscopy. We obtain a comprehensive explanation of the observed experimental signatures from a model of polydisperse hard spheres with additional weak attraction. In particular, the model predictions quantitatively describe the multiscale dynamical results from microscopic nanometer cage diffusion over mesoscopic micrometer gradient diffusion up to macroscopic viscosity. Based on a comparative discussion with results from other crystallin proteins, we suggest an interesting common pathway for dynamical arrest in all crystallin proteins, with potential implications for the understanding of crowding effects in the eye lens.

U2 - 10.1016/j.bpj.2020.10.035

DO - 10.1016/j.bpj.2020.10.035

M3 - Journal article

SN - 0006-3495

VL - 119

SP - 2483

EP - 2496

JO - Biophysical Journal

JF - Biophysical Journal

IS - 12

ER -