Curcumin promotes fibril formation in F isomer of human serum albumin via amorphous aggregation
| Autor: | Nivin Mothi, Avinash Kale, Basir Ahmad, Shivani A. Muthu |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Amyloid
Curcumin Globular protein Biophysics macromolecular substances Protein aggregation Fibril Biochemistry Protein Structure Secondary chemistry.chemical_compound Isomerism Microscopy Electron Transmission medicine Humans Benzothiazoles Serum Albumin chemistry.chemical_classification Protein Stability Circular Dichroism Organic Chemistry Temperature Human serum albumin Congo red Amorphous solid Protein Structure Tertiary Crystallography Kinetics Thiazoles chemistry medicine.drug Protein Binding |
| Zdroj: | Biophysical chemistry. 207 |
| ISSN: | 1873-4200 |
| Popis: | We here describe the amyloid fibrils promoting behavior of curcumin, which ability to inhibit amyloid fibrillization of several globular proteins is well documented. Transmission electron microscopy (TEM), 90° light scattering (RLS), thioflavine T (ThT) and Congo red (CR) binding studies demonstrated that both F (pH3.4) and E (pH1.8) isomers of human serum albumin (HSA) in the absence and presence of curcumin initially converted into amorphous aggregates. Interestingly, only the sample containing F isomer preincubated with curcumin formed fibrils on incubation for longer period. We also found that curcumin strongly bind to the F isomer, alter its secondary, tertiary structures and thermal stability. We conclude that the conversion of intermediate states into amorphous aggregate to fibrils is dictated by its conformation. This study provides unique insights into ligand-controlled HSA aggregation pathway and should provide a useful model system to study both amorphous and the fibrillar aggregation of multidomain proteins. |
| Databáze: | OpenAIRE |
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