dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:17:51Z
dc.date.accessioned2022-10-05T15:14:37Z
dc.date.available2014-05-20T14:17:51Z
dc.date.available2022-10-05T15:14:37Z
dc.date.created2014-05-20T14:17:51Z
dc.date.issued2010-01-01
dc.identifierQuímica Nova. Sociedade Brasileira de Química, v. 33, n. 4, p. 841-845, 2010.
dc.identifier0100-4042
dc.identifierhttp://hdl.handle.net/11449/25350
dc.identifier10.1590/S0100-40422010000400014
dc.identifierS0100-40422010000400014
dc.identifierWOS:000278322500014
dc.identifierS0100-40422010000400014.pdf
dc.identifier5711182251641103
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3898465
dc.description.abstractToxin-antitoxin (TA) systems contribute to plasmid stability by a mechanism called post-segregational killing. The ccd was the first TA system to be discovered with CcdB being the toxin and CcdA the antitoxin. CcdA, an 8.3 kDa protein, interacts with CcdB (11.7 kDa), preventing the cytotoxic activity of CcdB on the DNA gyrase. As an approach to understanding this interaction, CcdA41, a polypeptide derived from CcdA, was synthesized by solid-phase methodology and its interaction with CcdB was analyzed by steady state fluorescence. CcdA41 formed a stable complex with CcdBET2, a peptide based on CcdB, the more recently described bacterial topoisomerase inhibitor.
dc.languagepor
dc.publisherSociedade Brasileira de Química
dc.relationQuímica Nova
dc.relation0.646
dc.relation0,255
dc.rightsAcesso aberto
dc.sourceSciELO
dc.subjectbacterial toxin
dc.subjectpeptides
dc.subjectfluorescence
dc.titleSíntese, caracterização e estudos de interação de um análogo da antitoxina CcdA empregando fluorescência no estado estacionário
dc.typeArtigo


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