Study on Interaction between 5-Bromo-4-thio-2'-deoxyuridine and human serum albumin by spectroscopy and molecular docking

Spectrochim Acta A Mol Biomol Spectrosc. 2015 Feb 5:136 Pt C:1775-81. doi: 10.1016/j.saa.2014.10.081. Epub 2014 Oct 30.

Abstract

The interaction between 5-Bromo-4-thio-2'-deoxyuridine (4-SBrdU) and human serum albumin (HSA) was investigated by the methods of UV-vis absorbance, fluorescence and circular dichroism (CD) spectroscopy and molecular docking under simulative physiological conditions. The results showed that the quenching mechanism of HAS by 4-SBrdU was dynamic fluorescence quenching, hydrophobic interaction was the main intermolecular force based on thermodynamic data, the fluorescence experimental results were in agreement with results obtained by the molecular docking study.

Keywords: 5-Bromo-4-thio-2′-deoxyuridine (4-SBrdU); Fluorescence spectroscopy; Human serum albumin (HSA); Molecular docking; Nucleoside.

MeSH terms

  • Binding Sites
  • Bromodeoxyuridine / chemistry
  • Bromodeoxyuridine / pharmacokinetics
  • Circular Dichroism
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Docking Simulation
  • Protein Binding
  • Protein Conformation
  • Serum Albumin, Human / chemistry*
  • Serum Albumin, Human / metabolism*
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet
  • Thiouridine / analogs & derivatives
  • Thiouridine / chemistry
  • Thiouridine / pharmacokinetics

Substances

  • Thiouridine
  • 4-thio-2'-deoxyuridine
  • Bromodeoxyuridine
  • Serum Albumin, Human