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AZT binding to Na,K-ATPase.

A Ahmed-Ouameur1, J-F Neault, S Claveau

  • 1Department of Chemistry-Biology, University of Québec at Trois-Riviéres, C.P. 500, TR (Québec) Canada G9A 5H7.

Cell Biochemistry and Biophysics
|January 28, 2005
PubMed
Summary
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3'-azido-3'-deoxythymidine (AZT), an HIV drug, interacts with Na,K-ATPase. At low concentrations, AZT binds via hydrogen bonds, while higher concentrations form AZT-lipid complexes, causing minor protein structure changes.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • 3'-azido-3'-deoxythymidine (AZT) is a primary drug for treating human immunodeficiency virus (HIV).
  • Drug interactions with DNA and proteins are crucial for understanding its in vivo mechanism of action.

Purpose of the Study:

  • To investigate the interaction between AZT and Na,K-ATPase.
  • To characterize the binding mode, binding constants, and effects on protein secondary structure.

Main Methods:

  • Utilized ultraviolet absorption and Fourier transform infrared (FTIR) difference spectroscopy.
  • Employed self-deconvolution, second-derivative resolution enhancement, and curve-fitting techniques.
  • Studied interactions in both H2O and D2O solutions at physiological pH.

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Main Results:

  • At low AZT concentrations (0.1 microM), hydrogen bonding occurred with polypeptide C=O and C-N groups, yielding binding constants K1 = 5.3 x 10(5) M(-1) and K2 = 9.8 x 10(3) M(-1).
  • Higher AZT concentrations promoted AZT-lipid complex formation.
  • Minor alterations in protein secondary structure were observed at high AZT concentrations (1 mM), with changes in alpha-helix, beta-pleated, turn, beta-antiparallel, and random coil percentages.

Conclusions:

  • AZT exhibits concentration-dependent binding interactions with Na,K-ATPase.
  • These interactions involve hydrogen bonding at low concentrations and complex formation at high concentrations, leading to subtle modifications in protein secondary structure.