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Abstract
The denaturation of Bovine Serum Albumin (BSA) by a chaotropic agent, guanidinium hydrochloride (GuH(+)Cl(-)) was studied by fluorescence lifetime analysis. The BSA was labelled with 1-anilino-8-naphthalene sulfonate (ANS) at two different molar ratios (1:1) and (1:10). The non-exponential fluorescence kinetics of the BSA-ANS complex at different stages of denaturation is analysed using three different models: a discrete tri-exponential sum, stretched exponential, and Gaussian lifetime distribution. In all cases, the fluorescence decay times decreased with protein denaturation. The results from the models show that there are at least two different binding sites located in the BSA protein with different water accessibility.
| Original language | English (Ireland) |
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| Pages | 153-160 |
| Number of pages | 8 |
| DOIs | |
| Publication status | Published - 1 Mar 2006 |
| Event | 9th International Conference on Methods and Applications of Fluorescence: Spectroscopy, Imaging and Probes: MAF 9 - Lisbon, Portugal Duration: 4 Sep 2005 → 7 Sep 2005 https://link.springer.com/article/10.1007/s10895-006-0069-9 |
Conference
| Conference | 9th International Conference on Methods and Applications of Fluorescence: Spectroscopy, Imaging and Probes |
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| Country/Territory | Portugal |
| City | Lisbon |
| Period | 4/09/05 → 7/09/05 |
| Internet address |
Keywords
- 1-anilino-8-naphthalene sulfonate
- Bovine serum albumin
- Denaturation
- Fluorescence lifetime distribution
Authors (Note for portal: view the doc link for the full list of authors)
- Authors
- Togashi, D.M.; Ryder, A.G.;
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