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

Anna Rita Bizzarri1, Simona Santini1, Emilia Coppari1, Monica Bucciantini2, Silvia Di Agostino3, Tohru Yamada4, Craig W Beattie4, Salvatore Cannistraro11Biophysics and Nanoscience Centre, CNISM, Facolt&agrave; di Scienze, Universit&agrave; della Tuscia, Viterbo, 2Department of Bioche...

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Autores principales:	Bizzarri AR, Santini S, Coppari E, Bucciantini M, Di Agostino S, Yamada T, Beattie CW, Cannistraro S
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2011
Materias:	Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/71d1f5546f2d4710beee70d97e3fc574
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spelling	oai:doaj.org-article:71d1f5546f2d4710beee70d97e3fc5742021-12-02T00:54:54ZInteraction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy1176-91141178-2013https://doaj.org/article/71d1f5546f2d4710beee70d97e3fc5742011-11-01T00:00:00Zhttp://www.dovepress.com/interaction-of-an-anticancer-peptide-fragment-of-azurin-with-p53-and-i-a8732https://doaj.org/toc/1176-9114https://doaj.org/toc/1178-2013Anna Rita Bizzarri1, Simona Santini1, Emilia Coppari1, Monica Bucciantini2, Silvia Di Agostino3, Tohru Yamada4, Craig W Beattie4, Salvatore Cannistraro11Biophysics and Nanoscience Centre, CNISM, Facolt&agrave; di Scienze, Universit&agrave; della Tuscia, Viterbo, 2Department of Biochemical Sciences, University of Florence, Florence, 3Molecular Oncogenesis Laboratory, Experimental Oncology Department, Regina Elena Cancer Institute, Rome, Italy; 4Department of Surgical Oncology, University of Illinois College of Medicine, Chicago, IL, USAAbstract: 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.Keywords: AFS, cancer physics, unbinding forcesBizzarri ARSantini SCoppari EBucciantini MDi Agostino SYamada TBeattie CWCannistraro SDove Medical PressarticleMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol 2011, Iss default, Pp 3011-3019 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine (General) R5-920
spellingShingle	Medicine (General) R5-920 Bizzarri AR Santini S Coppari E Bucciantini M Di Agostino S Yamada T Beattie CW Cannistraro S Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
description	Anna Rita Bizzarri1, Simona Santini1, Emilia Coppari1, Monica Bucciantini2, Silvia Di Agostino3, Tohru Yamada4, Craig W Beattie4, Salvatore Cannistraro11Biophysics and Nanoscience Centre, CNISM, Facolt&agrave; di Scienze, Universit&agrave; della Tuscia, Viterbo, 2Department of Biochemical Sciences, University of Florence, Florence, 3Molecular Oncogenesis Laboratory, Experimental Oncology Department, Regina Elena Cancer Institute, Rome, Italy; 4Department of Surgical Oncology, University of Illinois College of Medicine, Chicago, IL, USAAbstract: 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.Keywords: AFS, cancer physics, unbinding forces
format	article
author	Bizzarri AR Santini S Coppari E Bucciantini M Di Agostino S Yamada T Beattie CW Cannistraro S
author_facet	Bizzarri AR Santini S Coppari E Bucciantini M Di Agostino S Yamada T Beattie CW Cannistraro S
author_sort	Bizzarri AR
title	Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
title_short	Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
title_full	Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
title_fullStr	Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
title_full_unstemmed	Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
title_sort	interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy
publisher	Dove Medical Press
publishDate	2011
url	https://doaj.org/article/71d1f5546f2d4710beee70d97e3fc574
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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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