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Studies on the binding affinity of anticancer drug mitoxantrone to chromatin, DNA and histone proteins

Zahra Hajihassan1, Azra Rabbani-Chadegani

  • 1Department of Biochemistry, Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. Hajihassan@ibb.ut.ac.ir

Journal of Biomedical Science
|March 17, 2009
PubMed

Insights

This study reveals that the anticancer drug mitoxantrone binds more strongly to chromatin than DNA. Histone proteins appear crucial for this enhanced binding of mitoxantrone to chromatin.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Mitoxantrone is a key chemotherapy agent for various cancers.
  • Understanding its interaction with cellular components like chromatin is vital for optimizing cancer therapy.

Purpose of the Study:

  • To compare the binding affinity of mitoxantrone to EDTA-soluble chromatin (SE-chromatin), DNA, and histones.
  • To elucidate the role of histone proteins in mitoxantrone-chromatin interactions.

Main Methods:

  • UV/Vis spectroscopy
  • Fluorescence spectroscopy
  • Circular Dichroism (CD) spectroscopy
  • Gel electrophoresis
  • Equilibrium dialysis

Main Results:

  • Mitoxantrone induces compaction and aggregation of SE-chromatin, evidenced by hypochromicity and loss of DNA/histones on gels.
  • Strong interaction between mitoxantrone and histone proteins, causing structural changes.
  • Positive cooperative binding observed between mitoxantrone and chromatin.

Conclusions:

  • Mitoxantrone exhibits higher binding affinity for chromatin than for DNA.
  • Histone proteins likely play a significant role in mediating the interaction between mitoxantrone and chromatin.

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