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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Understanding curcumin-induced modulation of protein aggregation.
Basir Ahmad1, Mohanish S Borana2, Ankur P Chaudhary1
1Biophysical Chemistry & Structural Biology Laboratory, UM-DAE Centre for Excellence in Basic Sciences, University of Mumbai, Vidyanagari Campus, Mumbai 400098, India.
International Journal of Biological Macromolecules
|June 22, 2016
Summary
Curcumin, a compound from turmeric, can inhibit or promote protein aggregation and reduce aggregate toxicity. This review explores curcumin
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Protein aggregation is implicated in various diseases.
- Curcumin, from turmeric, shows potential in modulating protein aggregation.
- Understanding curcumin's molecular interactions is crucial for therapeutic development.
Purpose of the Study:
- To review the molecular mechanisms by which curcumin and its derivatives affect protein aggregation and toxicity.
- To elucidate the interaction between curcumin and proteins/peptides.
- To correlate curcumin's effects with aggregate structure and toxicity.
Main Methods:
- Analysis of curcumin-protein/peptide interactions.
- Investigation of effects on protein conformational stability and folding pathways.
- Examination of aggregation kinetics and mechanisms.
- Correlation of molecular interactions with aggregate toxicity.
Main Results:
- Curcumin interacts with proteins/peptides, influencing their stability and folding pathways.
- Curcumin binding affects aggregation kinetics, potentially inhibiting or promoting fibril formation.
- Curcumin can bind to intermediate species, altering the aggregation pathway.
- A correlation exists between curcumin-induced states and aggregate toxicity.
Conclusions:
- Curcumin's effect on protein aggregation is concentration- and context-dependent.
- A model for curcumin-mediated modulation of amyloid-like fibril formation is proposed.
- Curcumin's multifaceted interactions offer therapeutic potential for protein aggregation diseases.
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