ABSTRACT
The interaction between fasudil hydrochloride (FSD) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The Stern-Volmer quenching model has been successfully applied and the results revealed that FSD could quench the intrinsic fluorescence of BSA effectively via static quenching. The binding constants and binding sites for the BSA-FSD system were evaluated. The corresponding thermodynamic parameters obtained at different temperatures indicated that hydrophobic force played a major role in the interaction of FSD and BSA. The distance between the donor (BSA) and the acceptor (FSD) was obtained according to fluorescence resonance energy transfer (FRET). Synchronous fluorescence spectroscopy and FT-IR spectra showed that the conformation of BSA was changed in the presence of FSD. Copyright © 2015 John Wiley & Sons, Ltd.
Subject(s)
1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/analogs & derivatives , Serum Albumin, Bovine/chemistry , 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/chemistry , Animals , Cattle , Fluorescence Resonance Energy Transfer , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , ThermodynamicsABSTRACT
The interaction between Besifloxacin (BFLX) and bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-Vis absorption and circular dichroism) techniques under imitated physiological conditions. The experiments were conducted at different temperatures (298, 304 and 310 K) and the results showed that the BFLX caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained. The corresponding thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated at different temperatures. The results revealed that the binding process was spontaneous and the acting force between BFLX and BSA were mainly electrostatic forces. According to Förster non-radiation energy transfer theory, the binding distance between BFLX and BSA was calculated to be 4.96 nm. What is more, both synchronous fluorescence and circular dichroism spectra confirmed conformational changes of BSA.
Subject(s)
Azepines/metabolism , Fluoroquinolones/metabolism , Serum Albumin, Bovine/metabolism , Spectrum Analysis/methods , Animals , Azepines/chemistry , Cattle , Circular Dichroism , Fluoroquinolones/chemistry , Kinetics , Protein Binding , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , TemperatureABSTRACT
The interaction between 21-(Ph-NN)-NCTPP and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy under imitated physiological conditions. The results showed that the intrinsic fluorescence of BSA was quenched strongly by 21-(Ph-NN)-NCTPP. The binding constants (Ka) and the binding sites (n) were obtained at three different temperatures (298, 304, and 310K). The thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated, the results indicated that the binding process was spontaneous and the hydrophobic interaction played a major role in [21-(Ph-NN)-NCTPP]-BSA binding process. Based on the Förster non-radiation energy transfer theory, the binding distance from 21-(Ph-NN)-NCTPP to BSA was estimated to be about 3.51nm. What's more, the synchronous fluorescence spectra indicated that the conformation of BSA has not been changed.
Subject(s)
Porphyrins/metabolism , Serum Albumin, Bovine/metabolism , Animals , Binding Sites , Cattle , Energy Transfer , Hydrophobic and Hydrophilic Interactions , Protein Binding , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , ThermodynamicsABSTRACT
The interaction between novel spiro[cyclopropane-pyrrolizin] (NSCP) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy at 298 K, 304 K and 310 K under simulative physiological conditions. The results showed that NSCP can effectively quench the intrinsic fluorescence of BSA via static quenching. The binding constants, binding sites of NSCP with BSA were calculated. Hydrogen binds and van der Waals force played a major role in stabilizing the complex and the binding reaction were spontaneous. According to the Förster non-radiation energy transfer theory, the average binding distances between NSCP and BSA were obtained. What is more, the synchronous fluorescence spectra indicated that the conformation of BSA has been changed.
Subject(s)
Cyclopropanes/metabolism , Pyrroles/metabolism , Serum Albumin, Bovine/metabolism , Spiro Compounds/metabolism , Animals , Binding Sites , Cattle , Cyclopropanes/chemistry , Protein Binding , Pyrroles/chemistry , Serum Albumin, Bovine/chemistry , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , Spiro Compounds/chemistryABSTRACT
The interaction between carbonyl-fused N-confused porphyrin (CF-NCP) and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy. The results indicated that CF-NCP has strong ability to quench the intrinsic fluorescence of BSA by forming complexes. The binding constants (Ka), binding sites (n) were obtained. The corresponding thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated at three different temperatures. The results revealed that the binding process is spontaneous, and the acting force between CF-NCP and BSA were mainly electrostatic forces. According to Förster non-radiation energy transfer theory, the binding distance between CF-NCP and BSA was calculated to be 4.37nm. What is more, the conformation of BSA was observed from synchronous fluorescence spectroscopy.
