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ABSTRACT: Purpose
The significant lens chaperone protein α-crystallin (αABc), comprised of αA-crystallin (αAc) and αB-crystallin (αBc) subunits, is found to form membrane-bound aggregates with age and cataract formation. However, the molecular basis for such aggregate formation is still unclear. Our research primarily aims to elucidate the effect of lipids (phospholipids and sphingolipids) and cholesterol (Chol) peroxidation on the aggregation of αAc, αBc, and αABc to bovine lens nuclear membrane (NM).Methods
Lipid and Chol peroxidation was induced by a photosensitized peroxidation reaction, and topographical images of NM and oxidized-NM (Ox-NM) with and without αAc, αBc, or αABc were obtained using atomic force microscopy (AFM).Results
The percentage of membrane area occupie
SUBMITTER: Khadka NK
PROVIDER: S-EPMC12410278 | biostudies-literature | 2025 Sep
REPOSITORIES: biostudies-literature