Summary & Purpose

Several discoveries show that with age and cataract formation, B-crystallin binds with the lens membrane or associates with other lens proteins, which bind with the fiber cell plasma membrane, accompanied by light scattering and cataract formation. However, how lipids (phospholipids and sphingolipids) and cholesterol (Chol) influence B-crystallin binding to the membrane is unclear. This research aims to elucidate the role of lipids and Chol in the binding of B-crystallin to the membrane and the membrane’s physical properties (mobility, order, and hydrophobicity) with B-crystallin binding. We used electron paramagnetic resonance (EPR) spin-labeling methods to investigate the binding of BL-crystallin with a model of porcine lens-lipid (MPLL), model of mouse lens-lipid (MMLL), and model of human lens-lipid (MHLL) membrane with and without Chol. Our results show that BL-crystallin binds with all of the investigated membranes in a saturable manner and the maximum percentage of the membrane surface occupied (MMSO) by BL-crystallin and the binding affinity (Ka) of BL-crystallin to the membranes followed the trends: MMSO (MPLL) > MMSO (MMLL) > MMSO (MHLL) and Ka (MHLL) > Ka (MMLL) ˜ Ka (MPLL), respectively, in which the presence of Chol reduces the MMSO and Ka for all membranes. The mobility near the headgroup regions of the membranes decreases with an increase in the binding of BL-crystallin; however, the decrease is more pronounced in the MPLL and MMLL membranes than the MHLL membrane. In the MPLL and MMLL membranes, the membranes become slightly ordered near the headgroup with an increase in BL-crystallin binding compared to the MHLL membrane. The hydrophobicity near the headgroup region of the membrane increases with BL-crystallin binding; however, the increase is more pronounced in the MPLL and MMLL membranes than the MHLL membrane, indicating that BL-crystallin binding creates a hydrophobic barrier for the passage of polar molecules, which supports the barrier hypothesis in cataract formation. However, in the presence of Chol, there is no significant increase in hydrophobicity with BL-crystallin binding, suggesting that Chol prevents the formation of a hydrophobic barrier, possibly protecting against cataract formation.

Author Identifier

Geraline Torssi-Torres, ORCID: 0000-0002-1690-1562
Nawal K. Khadka, ORCID: 0000-0002-2404-3799
Raju Timsina, ORCID: 0000-0002-3790-8472
Laxman Mainali, ORCID: 0000-0002-9570-9041

Date of Publication or Submission

4-3-2025

DOI

https://doi.org/10.18122/biophysics_data.3.boisestate

Funding Citation

The research reported in this publication was supported by the National Eye Institute of the National Institutes of Health, under Award Number R01 EY030067. Support was provided, in part, by the National Institutes of Health, NIGMS, under grants no: P20GM103408 and P20GM109095, and the Biomolecular Research Center, RRID:SCR_019174, at Boise State University. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

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Series

Data Format

*.xlsx; *.txt

File Size

114KB

Data Attributes

See README file

Time Period

2020-2023

Update Frequency

Other

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