Alpha-Crystallin Association with the Model of Human and Animal Eye Lens-Lipid Membranes is Modulated by Surface Hydrophobicity of Membranes.
Autor: | Timsina R; Department of Physics, Boise State University, Boise, ID, USA., Trossi-Torres G; Biomolecular Sciences Graduate Program, Boise State University, Boise, ID, USA., Thieme J; Department of Physics, Boise State University, Boise, ID, USA., O'Dell M; Biomolecular Sciences Graduate Program, Boise State University, Boise, ID, USA., Khadka NK; Department of Physics, Boise State University, Boise, ID, USA., Mainali L; Department of Physics, Boise State University, Boise, ID, USA.; Biomolecular Sciences Graduate Program, Boise State University, Boise, ID, USA. |
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Jazyk: | angličtina |
Zdroj: | Current eye research [Curr Eye Res] 2022 Jun; Vol. 47 (6), pp. 843-853. Date of Electronic Publication: 2022 Mar 22. |
DOI: | 10.1080/02713683.2022.2040539 |
Abstrakt: | Purpose: This research aims to probe the interaction of α-crystallin with a model of human, porcine, and mouse lens-lipid membranes. Methods: Cholesterol/model of human lens-lipid (Chol/MHLL), cholesterol/model of porcine lens-lipid (Chol/MPLL), and cholesterol/model of mouse lens-lipid (Chol/MMLL) membranes with 0-60 mol% Chol were prepared using the rapid solvent exchange method and probe-tip sonication. The hydrophobicity near the surface of model lens-lipid membranes and α-crystallin association with these membranes were investigated using the electron paramagnetic resonance spin-labeling approach. Results: With increased Chol content, the hydrophobicity near the surface of Chol/MHLL, Chol/MPLL, and Chol/MMLL membranes, the maximum percentage of membrane surface occupied (MMSO) by α-crystallin, and the association constant ( K Conclusions: This study suggested that the interaction of α-crystallin with model lens-lipid membranes is hydrophobic. Furthermore, our data indicated that Chol and CBDs reduce α-crystallin association with lens membrane, likely increase α-crystallin concentration in lens cytoplasm, and possibly favor the chaperone-like activity of α-crystallin maintaining lens cytoplasm homeostasis. |
Databáze: | MEDLINE |
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