Dataset Information

Light-Induced Anti-Bacterial Effect Against Staphylococcus aureus of Porphyrin Covalently Bonded to a Polyethylene Terephthalate Surface.

ABSTRACT: Antimicrobial photodynamic inactivation represents a promising and potentially greener alternative to conventional antimicrobials, and a solution for multidrug-resistant strains. The current study reports the development and characterization of tetra-substituted diazirine porphyrin covalently bonded to polyethylene terephthalate (PET) and its use as an antimicrobial surface. The diazirine moiety on the porphyrin was activated using a temperature of 120 °C, which initiated a C-H insertion mechanism that irreversibly functionalized the PET surface. Activation of the surface with white LED light in phosphate-buffered saline (PBS) led to singlet oxygen generation, which was detected via the degradation of 9,10-anthracenediylbis(methylene)dimalonic acid (ADMA) over time. The bactericidal effect of the ¹O₂-producing surface against Staphylococcus aureus was determined qualitatively and quantitatively. The growth of the pathogen beneath porphyrin-functionalized PET coupons was reduced; moreover, the PET coupons resulted in a 1.76-log reduction in cell counts after exposure to white LED light for 6 h. This is a promising material and platform for the development of safer antimicrobial surfaces, with applications in healthcare, food packaging, marine surfaces, and other surfaces in the environment.

SUBMITTER: Musolino SF

PROVIDER: S-EPMC9404523 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature

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Light-Induced Anti-Bacterial Effect Against <i>Staphylococcus aureus</i> of Porphyrin Covalently Bonded to a Polyethylene Terephthalate Surface.

Musolino Stefania F SF Shatila Fatima F Tieman Grace M O GMO Masarsky Anna C AC Thibodeau Matthew C MC Wulff Jeremy E JE Buckley Heather L HL

ACS omega 20220810 33

Antimicrobial photodynamic inactivation represents a promising and potentially greener alternative to conventional antimicrobials, and a solution for multidrug-resistant strains. The current study reports the development and characterization of tetra-substituted diazirine porphyrin covalently bonded to polyethylene terephthalate (PET) and its use as an antimicrobial surface. The diazirine moiety on the porphyrin was activated using a temperature of 120 °C, which initiated a C-H insertion mechani ...[more]

PMID: 36033695

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Project description:Biodegradation of terephthalate (TPA) is a highly desired catabolic process for the bacterial utilization of this polyethylene terephthalate (PET) depolymerization product, but to date, the structure of terephthalate dioxygenase (TPDO), a Rieske oxygenase (RO) that catalyzes the dihydroxylation of TPA to a cis-diol, is unavailable. In this study, we characterized the steady-state kinetics and first crystal structure of TPDO from Comamonas testosteroni KF1 (TPDOKF1). TPDOKF1 exhibited substrate specificity for TPA (kcat/Km = 57 ± 9 mM-1 s-1). The TPDOKF1 structure harbors characteristic RO features as well as a unique catalytic domain that rationalizes the enzyme's function. The docking and mutagenesis studies reveal that its substrate specificity for TPA is mediated by the Arg309 and Arg390 residues, positioned on opposite faces of the active site. Additionally, residue Gln300 is also proven to be crucial for the activity, as its mutation to alanine decreases the activity (kcat) by 80%. This study delineates the structural features that dictate the substrate recognition and specificity of TPDO. IMPORTANCE Global plastic pollution has become the most pressing environmental issue. Recent studies on enzymes depolymerizing polyethylene terephthalate plastic into terephthalate (TPA) show some potential for tackling this. Microbial utilization of this released product, TPA, is an emerging and promising strategy for waste-to-value creation. Research in the last decade has identified terephthalate dioxygenase (TPDO) as being responsible for initiating the enzymatic degradation of TPA in a few Gram-negative and Gram-positive bacteria. Here, we determined the crystal structure of TPDO from Comamonas testosteroni KF1 and revealed that it possesses a unique catalytic domain featuring two basic residues in the active site to recognize TPA. Biochemical and mutagenesis studies demonstrated the crucial residues responsible for the substrate specificity of this enzyme.

Dataset Information

Light-Induced Anti-Bacterial Effect Against Staphylococcus aureus of Porphyrin Covalently Bonded to a Polyethylene Terephthalate Surface.

Publications

Light-Induced Anti-Bacterial Effect Against <i>Staphylococcus aureus</i> of Porphyrin Covalently Bonded to a Polyethylene Terephthalate Surface.

Similar Datasets

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