The Effects of Molecular Crowding on the Amyloid Fibril Formation of α-Lactalbumin and the Chaperone Action of α-Casein |
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Authors: | Arezou Ghahghaei Adeleh Divsalar Nasim Faridi |
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Institution: | (1) Department of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan, Iran;(2) Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran |
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Abstract: | Amyloid fibrils arise from the slow aggregation of intermediately folded protein states. In this study the kinetics of the
protein fibril formation of α-lactalbumin and its prevention by αS-casein in the presence and absence of the crowding agent,
dextran (68 kDa), have been compared using a thioflavin T binding assay. It was found that αS-casein, a molecular chaperone
found in bovine milk, is a potent in vitro inhibitor of α-lactalbumin fibrillization. The effect of αS-casein in preventing
fibril formation was significant, although less than it is in the absence of the crowding agent, dextran. The interaction
between the chaperone and the α-lactalbumin and structural change in the target protein are also shown using intrinsic fluorescence
intensity, an ANS binding assay, CD spectroscopy and size-exclusion HPLC. In summary, α-casein interacts with α-lactalbumin
and prevents amyloid formation but not as well as it does when the crowding agent, dextran, not present. |
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