Inhibitory Effect of β-Casein on the Amyloid Fibril Formation of Aβ1᾿0 Associated with Alzheimer's Disease
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- 作者：Arezou Ghahghaei ; Sima Shahraki
- 关键词：Alzheimer ; Amyloid fibril ; Chaperone ; β ; Casein ; Inhibition
- 刊名：International Journal of Peptide Research and Therapeutics
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：22
- 期：1
- 页码：23-29
- 全文大小：615 KB
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Zhang X, Fu X, Zhang H, Liu C, Jiao W, Chang Z (2005) Chaperone-like activity of β-casein. Int J Biochem Cell Biol 37:1232–1240CrossRef PubMed - 作者单位：Arezou Ghahghaei (1)
Sima Shahraki (1)
1. Department of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan, Iran - 刊物类别：Biomedical and Life Sciences
- 刊物主题：Life Sciences
Biochemistry
Animal Anatomy, Morphology and Histology
Polymer Sciences - 出版者：Springer Netherlands
- ISSN：1573-3904
文摘
Alzheimer’s disease is associated with the fibril formation of β-amyloid peptide in extracellular plaque. β-Casein is a milk protein that has shown a remarkable ability to stabilize proteins by inhibiting their protein aggregation and precipitation. The aim of this study was to test in vitro the ability of β-casein to bind the Aβ1–40, change the structure and inhibit the formation of amyloid fibrils in Aβ1–40. Results from the ThT binding assay indicated that incubation of Aβ1–40 with β-casein retarded amyloid fibril formation of Aβ1–40 in a concentration dependent manner such that at a ratio of 1:1 (w:w) led to a significant reduction in the amount of fluorescent intensity. The results from transmission electron microscopy (TEM) also showed that β-casein significantly reduced the number and size of the Aβ1–40 fibrils, suggesting that the chaperone bound to the Aβ1–40 fibrils and/or interacted with the fibrils in some way. ANS results also showed that β-casein significantly decreased the exposed hydrophobic surface in Aβ1–40. Following an ANS binding assay, CD spectroscopy results also showed that incubation of Aβ1–40 resulted in a structural transition to a β-sheet. In the presence of β-casein, however, α-helical conformation was observed which indicated stabilization of the protein. These results reveal the highly efficacious chaperone action of β-casein against amyloid fibril formation of Aβ1–40. These results suggest that in vitro, β-casein binds to the Aβ1–40 fibrils, alters the Aβ1–40 structure and prevents amyloid fibril formation. This approach may result in the identification of a chaperone mechanism for the treatment of neurological diseases.