Síntese, caracterização e estudos de interação de um análogo da antitoxina CcdA empregando fluorescência no estado estacionário
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/01/2010
|
Resumo |
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Processo FAPESP: 03/04492-3 Processo FAPESP: 07/08052-9 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. |
Formato |
841-845 |
Identificador |
http://dx.doi.org/10.1590/S0100-40422010000400014 Química Nova. Sociedade Brasileira de Química, v. 33, n. 4, p. 841-845, 2010. 0100-4042 http://hdl.handle.net/11449/25350 10.1590/S0100-40422010000400014 S0100-40422010000400014 WOS:000278322500014 S0100-40422010000400014.pdf |
Idioma(s) |
por |
Publicador |
Sociedade Brasileira de Química |
Relação |
Química Nova |
Direitos |
openAccess |
Palavras-Chave | #bacterial toxin #peptides #fluorescence |
Tipo |
info:eu-repo/semantics/article |