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Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-d-gluconate reductase A
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Nandini Sarkar
Veröffentlicht/Copyright:
27. Juni 2009
Abstract
We identified a molten globule-like intermediate of 2,5-diketo-d-gluconate reductase A (DKGR) at pH 2.5, which has a prominent β-sheet structure. The molten globule state of the protein shows amyloidogenic property >50 μm protein concentration. Interestingly, a 1:1 molar ratio of curcumin prevents amyloid formation as shown by the Thioflavin-T assay and atomic force microscopy. To the best of our knowledge, this is the first report on amyloid formation by an (α/β)8-barrel protein. The results presented here indicate that the molten globule state has an important role in amyloid formation and potential application of curcumin in protein biotechnology as well as therapeutics against amyloid diseases.
Received: 2009-4-16
Accepted: 2009-5-19
Published Online: 2009-06-27
Published in Print: 2009-10-01
©2009 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Guest Editorial
- Highlight: ‘Regenerative Hepatology’
- Highlight: Regenerative Hepatology
- The do's and don'ts of p53 isoforms
- Mechanisms of liver disease: cross-talk between the NF-κB and JNK pathways
- Immunologic hurdles of therapeutic stem cell transplantation
- Ancestral vascular tube formation and its adoption by tumors
- Cellular plasticity of the pancreas
- Hepatic and pancreatic stellate cells in focus
- Interplay between host cell and hepatitis C virus in regulating viral replication
- Epidermal growth factor receptor signaling in liver cell proliferation and apoptosis
- The chemokine scavenging receptor D6 limits acute toxic liver injury in vivo
- Hepatic differentiation of pluripotent stem cells
- Protein Structure and Function
- Effect of curcumin on amyloidogenic property of molten globule-like intermediate state of 2,5-diketo-d-gluconate reductase A
- Cell Biology and Signaling
- Specific induction of migration and invasion of pancreatic carcinoma cells by RhoC, which differs from RhoA in its localisation and activity
- Autoregulatory control of the p53 response by Siah-1L-mediated HIPK2 degradation
