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
Lingua originale | English |
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pagine (da-a) | 899-905 |
Numero di pagine | 7 |
Rivista | Biochemical and Biophysical Research Communications |
Volume | 354 |
Stato di pubblicazione | Published - 2007 |
All Science Journal Classification (ASJC) codes
- ???subjectarea.asjc.1300.1304???
- ???subjectarea.asjc.1300.1303???
- ???subjectarea.asjc.1300.1312???
- ???subjectarea.asjc.1300.1307???