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Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy

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Title: Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
Author(s): Bizzarri, Anna Rita; Santini, Simona; Coppari, Emilia; Bucciantini, Monica; Di Agostino, Silvia; Yamada, Tohru; Beattie, Craig W; Cannistraro, Salvatore
Subject(s): AFS cancer physics unbinding forces
Abstract: p28 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.
Issue Date: 2011-11-23
Publisher: Dove Medical Press
Citation Info: Bizzarri, 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.S26155
Type: Article
Description: This 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.S26155
URI: http://hdl.handle.net/10027/8554
ISSN: 1176-9114
Sponsor: This work was partly supported by a grant from the Italian Association for Cancer Research (AIRC No IG 10412).
Date Available in INDIGO: 2012-08-18
 

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