Pseudomonas aeruginosa azurin (Az)

Pseudomonas aeruginosa azurin is a 128-amino acid blue copper protein from the cupredoxin family that serves as an electron carrier in the respiratory chain of the bacterium [UniProt P00282]. It has gained significant attention in oncology because it selectively enters human cancer cells through an endocytic mechanism and induces apoptosis by binding to and stabilizing the p53 tumor suppressor protein [Yamada et al., 2002; Fialho et al., 2008]. This interaction prevents the MDM2-mediated degradation of p53, leading to cell cycle arrest and programmed cell death in various solid tumors [Chaudhari et al., 2017]. Additionally, azurin inhibits angiogenesis by interfering with the phosphorylation of vascular endothelial growth factor receptor 2 (VEGFR-2) and has demonstrated anti-parasitic and anti-viral properties [Fialho et al., 2008]. A fragment of the protein, a 28-amino acid peptide known as p28, has undergone clinical trials for the treatment of p53-expressing metastatic solid tumors and pediatric brain tumors, showing a favorable safety profile and potential efficacy without the DNA-damaging side effects typical of traditional chemotherapy [Lulla et al., 2016].

Other names

AzurinAzuBlue copper proteinPseudomonas copper protein

Azurin functions by entering cancer cells and forming a complex with the p53 tumor suppressor protein, thereby inhibiting the p53-MDM2 interaction and stabilizing p53 levels to induce apoptosis [Yamada et al., 2002]. It also inhibits the phosphorylation of VEGFR-2 to suppress angiogenesis [Fialho et al., 2008].