Molecular spectroscopic study on the interaction of tetracyclines with serum albumins

Spectrochim Acta A Mol Biomol Spectrosc. 2005 Feb;61(4):629-36. doi: 10.1016/j.saa.2004.05.028.

Abstract

A molecular spectroscopic investigation of the interaction between tetracyclines antibiotics and human serum albumin or bovine serum albumin was reported. The influences of some metal ions on the interaction were also studied. When tetracyclines drugs were added into the solution containing serum albumins, the fluorescence intensity of serum albumins decreased with the increasing of the drugs concentrations, which is due to the formation of new non-fluorescence complexes of drug-serum albumin. The tetracyclines acted as quenchers and quenched the fluorescence of the serum albumins. The binding constants and the number of the binding sites of the reaction of tetracyclines and serum albumins were obtained. The main sorts of acting force between the drugs and serum albumins were found and the action distances and the energy transfer efficiencies between donor-acceptor were calculated based on the Foster energy transference.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents / chemistry
  • Calcium / chemistry
  • Cattle
  • Chlortetracycline / pharmacology
  • Copper / chemistry
  • Humans
  • Ions
  • Magnesium / chemistry
  • Models, Chemical
  • Models, Statistical
  • Oxytetracycline / pharmacology
  • Protein Binding
  • Serum Albumin / chemistry*
  • Serum Albumin, Bovine / chemistry
  • Spectrometry, Fluorescence
  • Spectrophotometry / methods*
  • Temperature
  • Tetracycline / chemistry
  • Tetracyclines / chemistry*
  • Thermodynamics
  • Zinc / chemistry

Substances

  • Anti-Bacterial Agents
  • Ions
  • Serum Albumin
  • Tetracyclines
  • Serum Albumin, Bovine
  • Copper
  • Tetracycline
  • Magnesium
  • Zinc
  • Calcium
  • Chlortetracycline
  • Oxytetracycline