Impact of binding to the multidrug resistance regulator protein LmrR on the photo-physics and -chemistry of photosensitizers

Sara H. Mejias*, Gerard Roelfes, Wesley R. Browne

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Light activated photosensitizers generate reactive oxygen species (ROS) that interfere with cellular components and can induce cell death, e.g., in photodynamic therapy (PDT). The effect of cellular components and especially proteins on the photochemistry and photophysics of the sensitizers is a key aspect in drug design and the correlating cellular response with the generation of specific ROS species. Here, we show the complex range of effects of binding of photosensitizer to a multidrug resistance protein, produced by bacteria, on the formers reactivity. We show that recruitment of drug like molecules by LmrR (Lactococcal multidrug resistance Regulator) modifies their photophysical properties and their capacity to induce oxidative stress especially in 1O2 generation, including rose bengal (RB), protoporphyrin IX (PpIX), bodipy, eosin Y (EY), riboflavin (RBF), and rhodamine 6G (Rh6G). The range of neutral and charged dyes with different exited redox potentials, are broadly representative of the dyes used in PDT.

Original languageEnglish
Pages (from-to)12228-12238
Number of pages11
JournalPPCP : Physical Chemistry Chemical Physics
Volume22
Issue number21
Early online date2020
DOIs
Publication statusPublished - 7-Jun-2020

Keywords

  • COUPLED ELECTRON-TRANSFER
  • PHOTODYNAMIC THERAPY
  • SINGLET OXYGEN
  • ROSE-BENGAL
  • EOSIN Y
  • ARTIFICIAL METALLOENZYMES
  • PROTOPORPHYRIN IX
  • OXIDATIVE STRESS
  • CYTOCHROME-C
  • RHODAMINE 6G

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