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Platinum complexes and pyruvate kinase activity

L Trynda1, D Kwiatkowska, W Tyran

  • 1Faculty of Chemistry, University of Wroclaw, Poland. ltl@wchuwr.chem.uni.wroc.pl

General Physiology and Biophysics
|July 24, 1998
PubMed
Summary

Platinum complexes like cis-DDP and potassium tetrachloroplatinate inhibit bovine heart pyruvate kinase (PK) activity. Platinum binding alters enzyme structure and increases resistance to denaturing agents.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Medicinal Chemistry

Background:

  • Pyruvate kinase (PK) is a crucial enzyme in glycolysis.
  • Platinum-based drugs are widely used in cancer chemotherapy.
  • Understanding platinum complex interactions with enzymes is vital for drug development.

Purpose of the Study:

  • To investigate the interaction between platinum complexes and bovine heart pyruvate kinase.
  • To determine the effect of platinum binding on PK activity and structure.
  • To elucidate the binding site and conformational changes induced by platinum.

Main Methods:

  • Absorption spectroscopy
  • Circular Dichroism (CD) spectroscopy
  • Fluorescence spectroscopy
  • Enzymic activity assays

Main Results:

  • Both cis-diamminedichloroplatinum(II) (cis-DDP) and potassium tetrachloroplatinate (K2PtCl4) reduced PK activity in a time- and concentration-dependent manner.
  • K2PtCl4 was more potent than cis-DDP in inhibiting PK activity.
  • Platinum binding caused alterations in the enzyme's secondary structure, indicated by changes in Cotton effects.
  • Fluorescence quenching of tryptophan residues suggested platinum binding near these sites.
  • Platinum-modified PK exhibited increased resistance to denaturation.

Conclusions:

  • Platinum complexes interact with bovine heart pyruvate kinase, leading to reduced enzymatic activity.
  • The interaction involves structural modifications, including changes in alpha-helical and beta-sheet content.
  • Platinum binding likely occurs at or near tryptophan residues.
  • The observed resistance to denaturing agents suggests a stabilizing effect of platinum binding on the enzyme's overall structure.

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