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 for this work

Research output: Contribution to journalJournal articleResearchpeer-review

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.
Original languageEnglish
JournalBiophysical Journal
Volume119
Issue number12
Pages (from-to)2483-2496
Number of pages14
ISSN0006-3495
DOIs
Publication statusPublished - 15 Dec 2020
Externally publishedYes

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