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RESEARCH PRODUCT

Trehalose effects on α-crystallin aggregates

V. G. NicolettiBruno PignataroClaudia CascioFrancesco AttanasioAnna SavarinoEnrico RizzarelliSalvatore Fisichella

subject

BiophysicsMicroscopy Atomic ForceBiochemistrythermal stabilitychemistry.chemical_compoundCrystallinNative stateThermal stabilityBenzothiazolesalpha-Crystallinsalpha-crystallinChaperone activityProtein Structure QuaternaryEye lensMolecular BiologyNative structureCircular DichroismTrehalosefood and beveragesCell BiologyTrehaloseeye diseaseschaperone activityThiazolesSpectrometry FluorescencechemistryBiochemistryaggregatesα-Crystallin Trehalose Aggregates Chaperone activity Thermal stabilitysense organs

description

alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on alpha-crystallin aggregates. The role of trehalose in alpha-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the alpha-crystallin native structure, inhibits alpha-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone activity. (c) 2007 Elsevier Inc. All rights reserved.

yearjournalcountryeditionlanguage
2007-01-01Biochemical and Biophysical Research Communications
https://doi.org/10.1016/j.bbrc.2007.01.061