Candesartan, losartan and valsartan Zn(II) complexes interactions with bovine serum albumin

Future Med Chem. 2022 Jan;14(1):9-16. doi: 10.4155/fmc-2021-0216. Epub 2021 Nov 3.

Abstract

Background: The pharmacological response and the therapeutic efficacy of a drug depends on the interactions with plasma proteins. Methodology: The interaction of bovine serum albumin (BSA) with the metal complexes of antihypertensive drugs, Zn(II)/sartan complexes (candesartan, valsartan and losartan), was investigated using fluorescence quenching determinations at different temperatures. Results: The binding studies of the compounds with BSA showed static quenching and moderate binding with calculated constants in the range of 104-106 M-1, indicating potent serum distribution via albumins. In all cases, negative values of free energy are indicative of spontaneous processes and the stabilization of BSA/compound complexes through hydrogen bonding and van der Waals forces. The results for the sartans agree with the reported pharmacokinetics studies. Conclusion: It has been determined that the three sartans and the Zn complexes could be transported and distributed by albumin.

Keywords: Zn(II) metal complex; angiotensin II receptor blockers; bovine serum albumin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Benzimidazoles / chemistry*
  • Biphenyl Compounds / chemistry*
  • Cattle
  • Coordination Complexes / chemistry
  • Coordination Complexes / metabolism*
  • Kinetics
  • Losartan / chemistry*
  • Protein Binding
  • Serum Albumin, Bovine / chemistry
  • Serum Albumin, Bovine / metabolism*
  • Spectrophotometry
  • Temperature
  • Tetrazoles / chemistry*
  • Thermodynamics
  • Valsartan / chemistry*
  • Zinc / chemistry*

Substances

  • Benzimidazoles
  • Biphenyl Compounds
  • Coordination Complexes
  • Tetrazoles
  • Serum Albumin, Bovine
  • Valsartan
  • Zinc
  • Losartan
  • candesartan