The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.

α-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 cataractogene...

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Autores principales:	Giuseppe Maulucci, Massimiliano Papi, Giuseppe Arcovito, Marco De Spirito
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/43afa2aea000458982e379eaffbebab5
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spelling	oai:doaj.org-article:43afa2aea000458982e379eaffbebab52021-11-18T06:54:15ZThe thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.1932-620310.1371/journal.pone.0018906https://doaj.org/article/43afa2aea000458982e379eaffbebab52011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21573059/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203α-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 α-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 Tc, 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 α-crystallin in protecting from aggregation and preserving the transparency of the lens under hyperthermic conditions.Giuseppe MaulucciMassimiliano PapiGiuseppe ArcovitoMarco De SpiritoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e18906 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Giuseppe Maulucci Massimiliano Papi Giuseppe Arcovito Marco De Spirito The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
description	α-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 α-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 Tc, 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 α-crystallin in protecting from aggregation and preserving the transparency of the lens under hyperthermic conditions.
format	article
author	Giuseppe Maulucci Massimiliano Papi Giuseppe Arcovito Marco De Spirito
author_facet	Giuseppe Maulucci Massimiliano Papi Giuseppe Arcovito Marco De Spirito
author_sort	Giuseppe Maulucci
title	The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
title_short	The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
title_full	The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
title_fullStr	The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
title_full_unstemmed	The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
title_sort	thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/43afa2aea000458982e379eaffbebab5
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The thermal structural transition of α-crystallin inhibits the heat induced self-aggregation.

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