Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10767490 | Biochemical and Biophysical Research Communications | 2007 | 7 Pages |
Abstract
α-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 α-crystallin aggregates. The role of trehalose in α-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the α-crystallin native structure, inhibits α-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone activity.
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Authors
Francesco Attanasio, Claudia Cascio, Salvatore Fisichella, Vincenzo Giuseppe Nicoletti, Bruno Pignataro, Anna Savarino, Enrico Rizzarelli,