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Target Prediction of 5,10,15,20-Tetrakis(4'-Sulfonatophenyl)-Porphyrin Using Molecular Docking

Ana-Maria Udrea1,2, Andra Dinache1, Angela Staicu1

  • 1Laser Department, National Institute for Laser, Plasma and Radiation Physics, Atomistilor 409, 077125 Magurele, Romania.

Pharmaceutics
|November 11, 2022
PubMed

Insights

This study explores how a specific photosensitizer works in photodynamic therapy for cancer. It binds to key proteins like BCL-2, suggesting a potential mechanism for inhibiting cancer cell growth.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Photodynamic therapy (PDT) shows promise for cancer treatment.
  • The precise molecular mechanisms underlying PDT efficacy remain largely uncharacterized.
  • Understanding these mechanisms is crucial for developing more effective PDT strategies.

Purpose of the Study:

  • To investigate the molecular interactions of a specific photosensitizer used in PDT.
  • To predict the binding affinity of the photosensitizer with potential cancer-related protein targets.
  • To elucidate the potential molecular mechanisms of cancer cell inhibition by the photosensitizer.

Main Methods:

  • Utilized molecular docking simulations to predict binding affinities.
  • Employed UV-vis absorption spectroscopy to determine binding with human serum albumin.
  • Analyzed interactions with specific amino acid residues (HIS, MET) in target proteins.

Main Results:

  • The photosensitizer demonstrated binding affinity to several receptor targets, including B-cell lymphoma 2 (BCL-2), BCL-xL, MCL-1, and A1.
  • Binding interactions were predicted with HIS and MET amino acid residues in BCL-2, MCL-1, and β-catenin.
  • The photosensitizer also binds to human serum albumin, as confirmed by spectroscopy and docking.

Conclusions:

  • The studied porphyrin photosensitizer exhibits binding to human serum albumin.
  • Potential cancer cell inhibition may occur through interactions with BCL-2, MCL-1, and β-catenin receptors.
  • Low estimated free energy of binding with A1 and BCL-B receptors suggests alternative inhibitory pathways.
Keywords:
BCL-2 family proteinHSAPDTUV–vis absorption spectroscopybinding affinitycancer protein targetcancer therapyin silicomolecular docking

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