Journal Paper

Paper Information

Journal:
Year:0 | Volume: | Issue:
Start Page: | End Page:

video

sound

Persian Version

View:

18,551

Download:

0

Cites:

Information Journal Paper

Title

ABILITY OF QUERCETIN AND RUTIN TO CHANGE THE BINDING OF 6-MERCAPTOPURINE TO BOVINE SERUM ALBUMIN

Pages

 Start Page 107 | End Page 108

Abstract

 Binding of a drug to the serum albumins as major serum transport proteins can be influenced by other ligands leading to alteration of its pharmacological properties. In the present study, binding characteristics of 6-MERCAPTOPURINE (6-MP) with BOVINE SERUM ALBUMIN (BSA) together with its DISPLACEMENT from its binding site by QUERCETIN and RUTIN have been investigated by the spectroscopic method. According to the binding parameters, a static quenching component in overall dynamic quenching process is operative in the interaction between 6-MP and BSA. The binding of 6-MP to BSA occurred spontaneously due to entropy-driven hydrophobic interactions. The synchronous FLUORESCENCE SPECTROSCOPY study revealed that the secondary structure of BSA is changed in the presence of 6-MP and both Tyr and Trp residues participate in the interaction between 6-MP and BSA with the later one being more dominant. The binding constant value of 6-MP–BSA in the presence of QUERCETIN and RUTIN increased.6-MP was displaced by ibuprofen indicating that the binding site of 6-MP on albumin is site II. Therefore, the change of the pharmacokinetic and pharmacodynamic properties of 6-MP by QUERCETIN and RUTIN through alteration of binding capacity of 6-MP to the serum albumin cannot be ruled out. In addition, the DISPLACEMENT study showed that 6-MP is located in site II of BSA.

Cites

  • No record.
  • References

  • No record.
  • Related Journal Papers

  • No record.
  • Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops






    File Not Exists.