Abstract
The interaction between lanthanide cationic porphyrin and bovine serum albumin (BSA) was studied by fluorescence and UV-Vis spectrum. The static quenching of BSA was observed in the presence of YbTMPyP. According to the thermodynamic parameters, this binding was regarded as "enthalpy- driven" reaction. Furthermore, YbTMPyP is so close to the residues of BSA that molecular resonance energy transfer occurs between them. Besides, the red drift and hypochromicity of absorption spectrum of YbTMPyP were accompanied with the binding reaction.
| Original language | English |
|---|---|
| Pages (from-to) | 917-920 |
| Number of pages | 4 |
| Journal | Chinese Journal of Chemistry |
| Volume | 25 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2007 |
Scopus Subject Areas
- General Chemistry
User-Defined Keywords
- BSA
- Enthalpy-driven
- Fluorescence
- Hypochromicity
- Porphyrin