Alloxazine exhibits a range of bioactivities across various biological targets. It weakly inhibits platelet-derived growth factor receptor tyrosine kinase in Swiss 3T3 cells with an IC50 value exceeding 50,000 nM. The compound shows selective binding to human adenosine receptors, with Ki values of 935 nM for A2a, 3.8 nM for A2b, and over 100,000 nM for A1. Additionally, it displays high potency in inhibiting Lamin A splicing (0.9 nM) and various enzymes such as APE1, JMJD2E, HSD17B4, and ALDH1A1, among others.
Alloxazine exerts differential effects on the proliferation of Plasmodium falciparum and other targets including Caspase-7, Tyrosyl-DNA Phosphodiesterase, Cytochrome P450 2C19, Histone Lysine Methyltransferases, and multiple molecular interactions related to HIV-1, ELG1-dependent DNA repair, Marburg Virus and more. It demonstrates cytotoxicity in human THLE cells with an EC50 greater than 300,000 nM and induces reactive oxygen species with an EC50 of 226,000 nM. In antiviral activity assays, it inhibits SARS-CoV-2 cytotoxicity in VERO-6 cells with an IC50 value above 20,000 nM.
In cell viability assays, Alloxazine variably impacts different cell lines, enhancing growth in HEK293T cells but showing mixed or inhibitory effects on U2OS cells and human fibroblasts. Thermal Shift Assays reveal it affects protein thermal stability differently across diverse domains. Additionally, GPCR beta-arrestin recruitment assays indicate Alloxazine inhibits recruitment for several targets, including FFAR4, APLNR, AGTR1, and others..
Note: Summary generated by AI. Data source: ChEMBL 