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dc.contributor.authorBizzarri, Anna Rita
dc.contributor.authorSantini, Simona
dc.contributor.authorCoppari, Emilia
dc.contributor.authorBucciantini, Monica
dc.contributor.authorDi Agostino, Silvia
dc.contributor.authorYamada, Tohru
dc.contributor.authorBeattie, Craig W
dc.contributor.authorCannistraro, Salvatore
dc.date.accessioned2012-08-18T03:25:52Z
dc.date.available2012-08-18T03:25:52Z
dc.date.issued2011-11-23
dc.identifier.bibliographicCitationBizzarri, A. R., Santini, S., Coppari, E., Bucciantini, M., Di Agostino, S., Yamada, T., Beattie, C. W., & Cannistraro, S. 2011. Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy. International Journal of Nanomedicine, 6: 3011-3019. DOI: 10.2147/IJN.S26155en
dc.identifier.issn1176-9114
dc.identifier.otherDOI: 10.2147/IJN.S26155
dc.identifier.urihttp://hdl.handle.net/10027/8554
dc.descriptionThis is a copy of an article published in the International Journal of Nanomedicine © 2011 Bizzarri et al, publisher and licensee Dove Medical Press Ltd. This is an Open Access article which permits unrestricted noncommercial use, provided the original work is properly cited. DOI: 10.2147/IJN.S26155en
dc.description.abstractp28 is a 28-amino acid peptide fragment of the cupredoxin azurin derived from Pseudomonas aeruginosa that preferentially penetrates cancerous cells and arrests their proliferation in vitro and in vivo. Its antitumor activity reportedly arises from post-translational stabilization of the tumor suppressor p53 normally downregulated by the binding of several ubiquitin ligases. This would require p28 to specifically bind to p53 to inhibit specific ligases from initiating proteosome-mediated degradation. In this study, atomic force spectroscopy, a nanotechnological approach, was used to investigate the interaction of p28 with full-length p53 and its isolated domains at the single molecule level. Analysis of the unbinding forces and the dissociation rate constant suggest that p28 forms a stable complex with the DNA-binding domain of p53, inhibiting the binding of ubiquitin ligases other than Mdm2 to reduce proteasomal degradation of p53.en
dc.description.sponsorshipThis work was partly supported by a grant from the Italian Association for Cancer Research (AIRC No IG 10412).en
dc.language.isoen_USen
dc.publisherDove Medical Pressen
dc.subjectAFSen
dc.subjectcancer physicsen
dc.subjectunbinding forcesen
dc.titleInteraction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopyen
dc.typeArticleen


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