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
F ATTANASIO, C CASCIO, S FISICHELLA, V G NICOLETTI, PIGNATARO B, A SAVARINO, et al. (2007). Trehalose effects on a-crystallin aggregates. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 354(4), 899-905 [10.1016/j.bbrc.2007.01.061].
Trehalose effects on a-crystallin aggregates
CASCIO, Caterina;NICOLETTI, Valentina;PIGNATARO, Bruno Giuseppe;
2007-01-01
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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