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

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

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.

OriginalsprogEngelsk
TidsskriftBiophysical Journal
Vol/bind119
Udgave nummer12
Sider (fra-til)2483-2496
ISSN0006-3495
DOI
StatusUdgivet - 2020
Eksternt udgivetJa

Bibliografisk note

Funding Information:
We gratefully acknowledge financial support from the Knut and Alice Wallenberg Foundation (project grant KAW 2014.0052 ), the Swedish Research Council (VR; grants 2009-6794 , 2016-03301 and 2018-04627 ), the Faculty of Science at Lund University , the European Research Council ( ERC-339678-COMPASS ), the Royal Physiographic Society in Lund, and the Per-Eric and Ulla Schyberg’s Foundation . This work is based on experiments performed at the IN15 at the Institute Laue-Langevin, Grenoble, France ( 61 ).

Funding Information:
We thank Najet Mahmoudi for her help with sample preparation. We gratefully acknowledge financial support from the Knut and Alice Wallenberg Foundation (project grant KAW 2014.0052), the Swedish Research Council (VR; grants 2009-6794, 2016-03301 and 2018-04627), the Faculty of Science at Lund University, the European Research Council (ERC-339678-COMPASS), the Royal Physiographic Society in Lund, and the Per-Eric and Ulla Schyberg's Foundation. This work is based on experiments performed at the IN15 at the Institute Laue-Langevin, Grenoble, France (61).

Publisher Copyright:
© 2020 Biophysical Society

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