Spectroscopic studies on the interaction between Pr(III) complex of an ofloxacin derivative and bovine serum albumin or DNA
| Autor: | Liang Huang, Zhengzhi Zeng, Zhaorong Ma, Min Xu, Fengjuan Chen |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Ofloxacin
Spectrophotometry Infrared Absorption spectroscopy Intercalation (chemistry) Electrons Photochemistry Protein Structure Secondary Fluorescence spectroscopy Analytical Chemistry chemistry.chemical_compound Ethidium Animals Bovine serum albumin Binding site Spectroscopy Instrumentation Binding Sites Aqueous solution biology Viscosity Chemistry Potassium Iodide Titrimetry Serum Albumin Bovine DNA Atomic and Molecular Physics and Optics Kinetics Crystallography Spectrometry Fluorescence Energy Transfer biology.protein Cattle Salts Spectrophotometry Ultraviolet Hydroxyl radical Praseodymium Protein Binding |
| Zdroj: | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 78:503-511 |
| ISSN: | 1386-1425 |
| DOI: | 10.1016/j.saa.2010.11.018 |
| Popis: | The binding properties on [PrL2(NO3)](NO3)2 (L = 9-fluoro-2,3-dihydro-3-methyl-10-(4-methyl-1-piperaziny)-7-oxo-7Hpyrido[1,2,3-de]-1,4-benzoxazine-6-carbaldehyde benzoyl hydrazone) to bovine serum albumin (BSA) have been studied for the first time using fluorescence spectroscopy in combination with UV–Vis absorbance spectroscopy. The results showed that [PrL2(NO3)](NO3)2 strongly quenched the intrinsic fluorescence of BSA through a static quenching procedure, and non-radiation energy transfer happened within molecules. The number of binding site was about 1, and the efficiency of Forster energy transfer provided a distance of 4.26 nm between tryptophan and [PrL2(NO3)](NO3)2 binding site. At 288, 298, 310 K, the quenching constants of BSA–[PrL2(NO3)](NO3)2 system were 5.11 × 104, 4.33 × 104 and 3.71 × 104 l M−1. ΔH, ΔS and ΔG were obtained based on the quenching constants and thermodynamic theory (ΔH 0 and ΔG < 0). These results indicated that hydrophobic and electrostatic interactions are the mainly binding forces in the [PrL2(NO3)](NO3)2–BSA system. In addition, the CD spectra have proved that BSA secondary structure changed in the presence of [PrL2(NO3)](NO3)2 in aqueous solution. Moreover, the interaction between [PrL2(NO3)](NO3)2 and calf thymus DNA (CT DNA) was studied by spectroscopy and viscosity measurements, which showed that the binding mode of the [PrL2(NO3)](NO3)2 with DNA is intercalation. The DNA cleavage results show that in the absence of any reducing agent, the [PrL2(NO3)](NO3)2 can cleave plasmid pBR322 DNA and its hydrolytic mechanism was demonstrated with hydroxyl radical scavengers and singlet oxygen quenchers. |
| Databáze: | OpenAIRE |
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