Abstract
The binding of α-crystallin to the eye lens’s fiber cell plasma membrane increases with age and cataract. It has also been reported that the primary binding site of α-crystallin in the lens’s membrane is phospholipids (PLs). However, it is unclear whether PL acyl chain length and degree of unsaturation influence α-crystallin binding. We have used electron paramagnetic resonance spin-labeling methods to investigate the binding of α-crystallin with cholesterol (Chol)/phosphatidylcholine (PC) membrane of different chain lengths and degree of unsaturation (i.e., 14:0 PC, 18:0 18:1 PC, 18:1 PC, and 16:0 20:4 PC) and in the presence and absence of 23 mol% Chol.
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