Síntese, caracterização e estudos de interação de um análogo da antitoxina CcdA empregando fluorescência no estado estacionário

• Autor(a) principal: Cotrim, Camila Aparecida [UNESP]
• Data de Publicação: 2010
• Outros Autores: Garrido, Saulo Santesso [UNESP], Trovatti, Eliane [UNESP], Marchetto, Reinaldo [UNESP]
• Tipo de documento: Artigo
• Idioma: por
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1590/S0100-40422010000400014; http://hdl.handle.net/11449/25350
• topic: bacterial toxin; peptides; fluorescence

Toxin-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.