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Transporting testosterone and its dimers by serum proteins.

P Chanphai1, A R Vesper1, L Bekale1

  • 1Department of Chemistry, Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, Trois-Rivières, QC G9A 5H7, Canada.

Journal of Photochemistry and Photobiology. B, Biology
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PubMed
Summary

Steroids bind to serum proteins like human serum albumin (HSA) and bovine serum albumin (BSA), with testosterone showing the highest affinity. This binding, involving various interactions, alters protein structure and is a spontaneous process.

Keywords:
BindingModelingMorphologySerum albuminTEMTestosterone

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • A significant portion of steroids circulates in the blood bound to serum proteins.
  • Understanding steroid-protein interactions is crucial for comprehending their biological roles and pharmacokinetics.

Purpose of the Study:

  • To investigate the binding of testosterone and its dimers (aliphatic and aromatic) with human serum albumin (HSA) and bovine serum albumin (BSA).
  • To characterize the nature of steroid-protein interactions, protein aggregation, and conformational changes induced by steroid complexation.

Main Methods:

  • Multiple spectroscopic techniques (e.g., fluorescence, UV-Vis) were employed.
  • Transmission electron microscopy (TEM) was used to visualize protein morphology changes.
  • Molecular modeling and computational simulations were performed to analyze binding energies and interactions.

Main Results:

  • Steroids interact with serum albumin via hydrophobic, hydrophilic, and hydrogen bonding interactions.
  • Human serum albumin (HSA) forms more stable complexes than bovine serum albumin (BSA).
  • The binding affinity order was determined as testosterone > aromatic dimer > aliphatic dimer.
  • TEM revealed significant changes in protein aggregate diameter, indicating steroid encapsulation.
  • Molecular modeling confirmed spontaneous, hydrogen-bond-stabilized binding, with HSA exhibiting stronger binding (-12.95 kcal/mol) than BSA (-11.55 kcal/mol).
  • Steroid complexation induced greater conformational perturbations in BSA compared to HSA.

Conclusions:

  • Steroid binding to serum albumin is a spontaneous process driven by multiple interaction types.
  • HSA demonstrates higher affinity and stability in complex formation with steroids compared to BSA.
  • Steroid complexation significantly alters protein structure and morphology, influencing protein aggregation and conformation.