Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network
AbstractSurface Plasmon Resonance (SPR) is a powerful technique to study the kinetics of biomolecules undergoing biorecognition processes, particularly suited for protein-protein interactions of biomedical interest. The potentiality of SPR was exploited to sense the interactions occurring within the network of the tumor suppressor p53, which is crucial for maintaining genome integrity and whose function is inactivated, mainly by down regulation or by mutation, in the majority of human tumors. This study includes p53 down-regulators, p53 mutants and also the p53 family members, p63 and p73, which could vicariate p53 protective function. Furthermore, the application of SPR was extended to sense the interaction of p53 with anti-cancer drugs, which might restore p53 function. An extended review of previous published work and unpublished kinetic data is provided, dealing with the interaction between the p53 family members, or their mutants and two anticancer molecules, Azurin and its cell-penetrating peptide, p28. All the kinetic results are discussed in connection with those obtained by a complementary approach operating at the single molecule level, namely Atomic Force Spectroscopy and the related literature data. The overview of the SPR kinetic results may significantly contribute to a deeper understanding of the interactions within p53 network, also in the perspective of designing suitable anticancer drugs. View Full-Text
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Moscetti, I.; Cannistraro, S.; Bizzarri, A.R. Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network. Sensors 2017, 17, 2680.
Moscetti I, Cannistraro S, Bizzarri AR. Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network. Sensors. 2017; 17(11):2680.Chicago/Turabian Style
Moscetti, Ilaria; Cannistraro, Salvatore; Bizzarri, Anna R. 2017. "Surface Plasmon Resonance Sensing of Biorecognition Interactions within the Tumor Suppressor p53 Network." Sensors 17, no. 11: 2680.
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