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• W2984839545 endingPage "102122" @default.
• W2984839545 startingPage "102122" @default.
• W2984839545 abstract "The flavoenzyme D-amino acid oxidase (DAAO) represents a potentially good option for cancer enzyme prodrug therapy as it produces H2O2 using D-amino acids as substrates, compounds present at low concentration in vivo and that can be safely administered to regulate H2O2 production. We optimized the cytotoxicity of the treatment by: i) using an efficient enzyme variant active at low O2 and D-alanine concentrations (mDAAO); ii) improving the stability and half-life of mDAAO and the enhanced permeability and retention effect by PEGylation; and iii) inhibiting the antioxidant cellular system by a heme oxygenase-1 inhibitor (ZnPP). A very low amount of PEG-mDAAO (10 mU, 50 ng of enzyme) induces cytotoxicity on various tumor cell lines. Notably, PEG-mDAAO seems well suited for in vivo evaluation as it shows the same cytotoxicity at air saturation (21%) and 2.5% O2, a condition resembling the microenvironment found in the central part of tumors." @default.
• W2984839545 created "2019-11-22" @default.
• W2984839545 creator A5003169557 @default.
• W2984839545 creator A5088194056 @default.
• W2984839545 date "2020-02-01" @default.
• W2984839545 modified "2023-09-27" @default.
• W2984839545 title "PEG-DAAO conjugate: A promising tool for cancer therapy optimized by protein engineering" @default.
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• W2984839545 doi "https://doi.org/10.1016/j.nano.2019.102122" @default.
• W2984839545 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31706037" @default.
• W2984839545 hasPublicationYear "2020" @default.
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