Abstract
-crystallin, the major constituent of human lens, is a member of the heat-shock proteins family and it is known to have a quaternary structural transition at . The presence of calcium ions and/or temperature changes induce supramolecular self-aggregation, a process of relevance in the cataractogenesis. Here we investigate the potential effect of the bovine -crystallin's structural transition on the self-aggregation process. Along all the temperatures investigated, aggregation proceeds by forming intermediate molecular assemblies that successively aggregate in clusters. The final morphology of the aggregates, above and below , is similar, but the aggregation kinetics are completely different. The size of the intermediate molecular assemblies, and their repulsive energy barrier show a marked increase while crossing . Our results highlight the key role of heat modified form of -crystallin in protecting from aggregation and preserving the transparency of the lens under hyperthermic conditions.
Highlights
Cataract, the opacity of the eye lens, is an age-onset pathology that affects nearly 50% of the world’s population over the age of 65, and is the leading cause of blindness worldwide [1]
Pathological studies of cataractous lenses have revealed that cataracts are composed of protein aggregates that precipitate in eye lens cells
The increase in light scattering in old and cataractous lenses can be ascribed to alterations in lens crystallins interactions due to age related posttranslational modification of a-crystallin [5,6,7,8]
Summary
The opacity of the eye lens, is an age-onset pathology that affects nearly 50% of the world’s population over the age of 65, and is the leading cause of blindness worldwide [1].
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