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The Thermal Structural Transition of α-Crystallin Inhibits the Heat Induced Self-Aggregation

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  • Giuseppe Maulucci
  • Massimiliano Papi
  • Giuseppe Arcovito
  • Marco De Spirito

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.

Suggested Citation

  • Giuseppe Maulucci & Massimiliano Papi & Giuseppe Arcovito & Marco De Spirito, 2011. "The Thermal Structural Transition of α-Crystallin Inhibits the Heat Induced Self-Aggregation," PLOS ONE, Public Library of Science, vol. 6(5), pages 1-6, May.
    • Handle: RePEc:plo:pone00:0018906
    DOI: 10.1371/journal.pone.0018906
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