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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/25350
Title: 
Síntese, caracterização e estudos de interação de um análogo da antitoxina CcdA empregando fluorescência no estado estacionário
Other Titles: 
Synthesis, characterization and interaction studies of an analog of CcdA antitoxin by steady state fluorescence
Author(s): 
Institution: 
Universidade Estadual Paulista (UNESP)
ISSN: 
0100-4042
Sponsorship: 
  • Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
  • Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Sponsorship Process Number: 
  • FAPESP: 03/04492-3
  • FAPESP: 07/08052-9
Abstract: 
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.
Issue Date: 
1-Jan-2010
Citation: 
Química Nova. Sociedade Brasileira de Química, v. 33, n. 4, p. 841-845, 2010.
Time Duration: 
841-845
Publisher: 
Sociedade Brasileira de Química
Keywords: 
  • bacterial toxin
  • peptides
  • fluorescence
Source: 
http://dx.doi.org/10.1590/S0100-40422010000400014
URI: 
Access Rights: 
Acesso aberto
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/25350
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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