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Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c
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Structural Impact of 4-Hydroxynonenal Modification on Human Cytochrome CYP4F11.

Olena Gnatyuk1, Oleksii Skorokhod2, Alessandro Damin3

  • 1Institute of Physics, National Academy of Sciences of Ukraine, Kyiv, Ukraine.

Chemmedchem
|January 31, 2026
PubMed
Summary

Lipid peroxidation product 4-hydroxynonenal (4-HNE) alters human enzyme CYP4F11 structure. This protein lipoxidation impacts enzyme function, potentially affecting lipid metabolism and detoxification processes.

Keywords:
4‐hydroxynonenal (4‐hNE)CYP4F11Fourier transform infrared (FTIR) spectroscopyP450differential scanning calorimetrylipid peroxidationluminescencepost‐translational protein modificationsraman spectroscopy

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Posttranslational modifications of human enzymes are critical in disease pathogenesis.
  • 4-hydroxynonenal (4-HNE), a product of lipid peroxidation, modifies proteins, disrupting their function.
  • Human cytochrome CYP4F11, involved in lipid metabolism and xenobiotic degradation, is inhibited by 4-HNE.

Purpose of the Study:

  • To investigate the structural changes in human cytochrome CYP4F11 induced by 4-hydroxynonenal (4-HNE) modification.
  • To understand how protein lipoxidation affects CYP4F11 structure and function.

Main Methods:

  • Differential scanning calorimetry (DSC) to assess thermal stability and unfolding.
  • Fourier transform infrared (FTIR) and Raman spectroscopy to analyze secondary structure and molecular changes.
  • Computational analysis to support spectroscopic data interpretation.

Main Results:

  • DSC revealed an increased energetic barrier to unfolding, indicating structural reorganization.
  • FTIR analysis showed a decrease in alpha-helix content and an increase in beta-structure.
  • Raman spectroscopy detected significant alterations in luminescence decay, suggesting changes in the protein environment.

Conclusions:

  • 4-HNE conjugation induces significant structural alterations in CYP4F11, including changes in secondary structure.
  • These structural modifications may influence the enzymatic activity of CYP4F11.
  • The findings have potential implications for understanding lipid metabolism and xenobiotic detoxification in disease contexts.