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Proteins from Avastin® (bevacizumab) show tyrosine nitrations for which the consequences are completely unclear

Jia Wan1, Edina Csaszar, Wei-Qiang Chen

  • 1Department of Pediatrics, Medical University of Vienna, Vienna, Austria.

Plos One
|April 24, 2012
PubMed

Insights

This study investigated posttranslational modifications in Avastin (bevacizumab), a cancer drug. Researchers discovered tyrosine nitration on Avastin

Area of Science:

  • Proteomics
  • Biochemistry
  • Pharmaceutical Science

Background:

  • Avastin (bevacizumab) is a widely used protein drug for cancer therapy.
  • Serious side effects raise questions about its continued use.
  • No systematic proteomic studies on Avastin's posttranslational modifications (PTMs) have been reported.

Purpose of the Study:

  • To conduct a systematic proteomic analysis of Avastin to identify PTMs.
  • To investigate potential causes of Avastin's adverse effects.
  • To assess the impact of PTMs on Avastin's function and safety.

Main Methods:

  • Two-dimensional gel electrophoresis (2-DE) for protein separation.
  • Multi-enzyme in-gel digestion for peptide generation.
  • Mass spectrometry (nano-LC-ESI-MS/MS; HCT and LTQ Orbitrap MS) for peptide and PTM identification.

Main Results:

  • Bevacizumab heavy and light chains were identified with high sequence coverage.
  • Multiple tyrosine nitrations were detected on both chains, appearing as nitrotyrosine or aminotyrosine.
  • Aminotyrosine formation from nitrotyrosine under reducing conditions was observed.

Conclusions:

  • Tyrosine nitration is a significant PTM present in Avastin.
  • This nitration may contribute to the adverse effects associated with Avastin therapy.
  • Nitration of Avastin presents a challenge for pharmaceutical production and quality control.

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