Study of characterization and application on the binding between 5-IODOURIDINE (cas 1024-99-3) with HSA by spectroscopic and modeling

Add time:07/21/2019    Source:sciencedirect.com

The binding of 5-IODOURIDINE (cas 1024-99-3) with human serum albumin was investigated under the simulative physiological conditions. The fluorescence spectra in combination with UV absorption and modeling method were used in the present work. A strong fluorescence quenching reaction of 5-iodouridine to HSA was observed and the quenching mechanism was suggested as static quenching procedure. The binding constants (K) at different temperatures as well as thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated. It showed that the hydrophobic interaction was a predominant intermolecular force in order to stabilize the complex, which was in agreement with the result of modeling study. The binding distance between 5-iodouridine and HSA was calculated on the basis of the theory of Föster energy transfer. The effects of other ions on the binding constants were also discussed. Synchronous fluorescence spectroscopy (SFS) technique were successfully applied to determine protein in the biological samples.

We also recommend Trading Suppliers and Manufacturers of 5-IODOURIDINE (cas 1024-99-3). Pls Click Website Link as below: cas 1024-99-3 suppliers

Prev:Efficient esterification of carboxylic acids and phosphonic acids with trialkyl orthoacetate in ionic liquid
Next:Design and synthesis of 3-aminophthalazine derivatives and structural analogues as PDE5 inhibitors: anti-allodynic effect against neuropathic pain in a mouse model)