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


Autoria(s): Cotrim, Camila Aparecida; Garrido, Saulo Santesso; Trovatti, Eliane; Marchetto, Reinaldo
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

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