Synthesis, characterization and interaction studies of an analog of CcdA antitoxin by steady state fluorescence

Author(s)

Camila Aparecida Cotrim ^[1] ; Saulo Santesso Garrido ^[2] ; Eliane Trovatti ^[3] ; Reinaldo Marchetto ^[4]

Affiliation

^[1] Universidade Estadual Paulista. Instituto de Química. Departamento de Bioquímica e Tecnologia Química - Brasil

^[2] Universidade Estadual Paulista. Instituto de Química. Departamento de Bioquímica e Tecnologia Química - Brasil

^[3] Universidade Estadual Paulista. Instituto de Química. Departamento de Bioquímica e Tecnologia Química - Brasil

^[4] Universidade Estadual Paulista. Instituto de Química. Departamento de Bioquímica e Tecnologia Química - Brasil

• Document type: Journal article
• Source: Química Nova; v. 33, n. 4, p. 841-845, 2010-00-00.

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. (AU)

• FAPESP's process: 07/08052-9 - Studies of inhibition of the bacterial topoisomerases activity by CcdB analogues and the antidote effect of the CcdA41 peptide
• Grantee: Camila Aparecida Cotrim
• Support Opportunities: Scholarships in Brazil - Scientific Initiation