Piecemeal Rekindling of Coumarin 6 Fluorescence on Stepwise Unfolding of Protein by Surfactant
| Autor: | Rajashree Banerjee, Pradipta Purkayastha |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Serum albumin
02 engineering and technology 010402 general chemistry 01 natural sciences Micelle Fluorescence chemistry.chemical_compound Surface-Active Agents Pulmonary surfactant Coumarins Materials Chemistry Molecule Animals Physical and Theoretical Chemistry Bovine serum albumin Protein Unfolding biology Chemistry Serum Albumin Bovine 021001 nanoscience & nanotechnology Coumarin 0104 chemical sciences Surfaces Coatings and Films Thiazoles Spectrometry Fluorescence biology.protein Biophysics Cattle 0210 nano-technology Hydrophobic and Hydrophilic Interactions Vicinal |
| Zdroj: | The journal of physical chemistry. B. 121(51) |
| ISSN: | 1520-5207 |
| Popis: | Coumarin 6 (C6) briskly aggregates in water, and as a result, rapidly loses fluorescence. However, vicinal hydrophobic cavity can induce disintegration of the aggregates, and thus reviving the fluorescence. It is shown that carrier protein, such as bovine serum albumin (BSA), can disintegrate the microcrystals of C6 to smaller fragments and trap them inside the hydrophobic domain of the folded protein. This results into a 12-fold enhancement in the fluorescence signal of C6. However, on unfolding BSA by micelles, the C6 microcrystals break into single molecules by getting trapped in the micelles, and hence emission enhances by more than 100-folds. |
| Databáze: | OpenAIRE |
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