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Provedor de dados:  Anais da ABC (AABC)
País:  Brazil
Título:  Copper II - polar amino acid complexes: toxicity to bacteria and larvae of Aedes aegypti
Autores:  RODRIGUES,THIAGO A.D.
ARRUDA,EDUARDO J. DE
FERNANDES,MAGDA F.
CARVALHO,CLAUDIO T. DE
LIMA,ALESSANDRA R.
CABRINI,ISAÍAS
Data:  2017-01-01
Ano:  2017
Palavras-chave:  Neurotransmitter
Bacteria
Population control of vectors
Metal-insecticide
Mosquito
Resumo:  ABSTRACT Control strategies using insecticides are sometimes ineffective due to the resistance of the insect vectors.In this scenario new products must be proposed for the control of insect vectors.The complexes L-aspartate Cu (II) and L-glutamate-Cu (II) complexes were synthesized and characterized by elemental analysis, visible ultraviolet, infrared spectroscopy and potentiometric titration. The toxicity of these complexes was analyzed in Aedes aegypti (Diptera: Culicidae) larvae and Gram-negative and Gram-positive bacteria. The interaction between the ligands and the amino acid balance and the distribution of the species as a function of pH were discussed. The lethal concentration median (LC50) for Ae. aegypti larvae were: L-glutamic acid-Cu (II) - 53.401 mg L-1 and L-aspartate-Cu (II) - 108.647 mg L-1. The minimum inhibitory concentration (MIC) required for Staphylococcus aureus and Escherichia coli was: L-glutamate-Cu (II) 500-2000 mg L-1 and L-aspartate-Cu (II) 1000-2000 mg L-1. The concentrations demonstrated toxicity that evidence the potential of the complexes as bactericide and insecticide. Metal complexes formed by amino acids and transition metals are advantageous because of low environmental toxicity, biodegradability and low production cost.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652017000502273
Editor:  Academia Brasileira de Ciências
Relação:  10.1590/0001-3765201720160775
Formato:  text/html
Fonte:  Anais da Academia Brasileira de Ciências v.89 n.3 suppl.0 2017
Direitos:  info:eu-repo/semantics/openAccess
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