Protein binding of methohexital. Study of parameters and modulating factors using the equilibrium dialysis technique

Study on the interaction between theasinesin and human serum albumin by fluorescence spectroscopy

“…There are some works to study the interaction of drug with protein by fluorescence spectroscopy [16,17], UV-spectrophotometry [18], circular dichroism spectroscopy (CD) [19], electrochemistry [20], equilibrium dialysis [21], attenuated total reflectance-Fourier transform infrared (ATR-FTIR) [22], Raman spectroscopy [23], nuclear magnetic resonance (NMR) [24]. Fluorescence quenching is a powerful method to study the molecular interactions involving proteins because it is sensitive, rapid and relatively easy to use.…”

Equilibrium sampling through membrane based on a single hollow fibre for determination of drug–protein binding and free drug concentration in plasma

“…These include affinity chromatography [5], ultrafiltration [6], ultracentrifugation [3], equilibrium dialysis [7], microdialysis [8], capillary electrophoresis [9] solvent microextraction [10] and supported liquid membrane extraction [11,12]. These methods differ in their speed, data quality and complexity [13].…”

Determination of unbound drug concentration and protein-drug binding fraction in plasma

“…Plasma and buffer are filled in their respective compartment and drug equilibrium is built up between plasma and buffer. Equilibrium dialysis has been used for determining the protein-bound factions of drugs, such as methohexibal (Girard and Ferry, 1996), tri-iodothyrine (Klee, 1996), and benzoic and phenylacetic acid derivatives (Laznicek and Laznickova, 1995). This method, however, has many problems, including volume shifts, Donnan effects, loss of drug due to non-specific adsorption and difficulty in the control of some experimental variables (Oravcova et al, 1996); it is also time consuming and this makes the method inapplicable to unstable drugs in dialysis medium.…”