Fluorescence resonance energy transfer from tryptophan to folic acid in micellar media and deionised water.

The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueous sodiumdodecyl sulphate, cetyltrimethyl ammonium bromide, and Brij-35 as well as deionised water was investigated using steady state and time resolved fluorescence techniques. The data obtained from steady state fluorescence spectral studies and time resolved measurement indicated that the FRET from Trp to FA occurred most effectively in aqueous sodium dodecyl sulphate micellar solutions. The distance between Trp and FA were evaluated. Binding constant, number of binding sites and thermodynamic parameters were determined for Trp-FA interactions in deionised water. The values of the thermodynamic parameters suggest that the hydrophobic forces and hydrogen bonding are the key interacting forces between Trp-FA interaction.

Interaction between felodipine and bovine serum albumin: fluorescence quenching study.

The fluorescence quenching spectrum of bovine serum albumin (BSA) was investigated in the presence of felodipine (FLD) by spectroscopic methods including fluorescence spectroscopy and UV-Vis absorption spectroscopy. Stern-Volmer quenching was successfully applied and the corresponding thermodynamic parameters, namely enthalpy change (DeltaH), free energy change (DeltaG) and entropy change (DeltaS) at different temperatures (304, 314 and 324 K) were calculated according to the Van't Hoff relation. This revealed that the hydrophobic interaction plays a major role in stabilizing the complex. The fluorescence spectrum of BSA was studied in presence of various concentrations of SDS surfactant. The distance (r) between donor (BSA) and acceptor (FLD) was obtained according to fluorescence resonance energy transfer (FRET). The synchronous fluorescence spectroscopy was used to investigate the effect of FLD on BSA molecule. The result shows that the conformation of BSA was changed in the presence of felodipine.

Spectroscopic studies on the interaction between norfloxacin and p-amino benzoic acid: analytical application on determination of norfloxacin.

Fluorescence (Förster) Resonance Energy Transfer (FRET) between norfloxacin (NF) and p-amino benzoic acid (PABA) has been investigated by fluorescence and UV-vis absorption spectroscopy. It was found that the quenching of fluorescence of PABA is followed by simultaneous sensitization of NF fluorescence. The hydrophobic and electrostatic interaction plays an important role to stabilize the complex. The binding constant (K), binding site number (n) and corresponding thermodynamic parameters like free energy change (DeltaG), enthalpy change (DeltaH) and entropy change (DeltaS) were determined according to van't Hoff equation. Using FRET, the distance (r) between donor (PABA) and acceptor (NF) was obtained. This method is simple, selective and relatively free of interference from co-existing substances. The method was successfully applied to the determination of norfloxacin from pharmaceutical tablets.