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Insecticidal activity of Leptodactylus knudseni andPhyllomedusa vaillantii crude skin secretions against the mosquitoes Anopheles darlingi andAedes aegypti J. Venom. Anim. Toxins incl. Trop. Dis.
Trindade,Frances TT; Soares,Ângela A; Moura,Andréa A de; Rego,Tiago B; Soares,Andreimar M; Stábeli,Rodrigo G; Calderon,Leonardo A; Almeida e Silva,Alexandre de.
Background Mosquitoes are important vectors of several diseases, including malaria and dengue, and control measures are mostly performed using chemical insecticides. Unfortunately, mosquito resistance to commonly applied insecticides is widespread. Therefore, a prospection for new molecules with insecticidal activity based on Amazon biodiversity using the anuransLeptodactylus knudseni andPhyllomedusa vaillantii was performed against the mosquito speciesAnopheles darlingi and Aedes aegypti.Methods The granular secretion from anuran skin was obtained by manual stimulation, and lethal concentrations (LCs) for larvicidal and adulticidal tests were calculated using concentrations from 1-100 ppm. The skin secretions from the anuran species tested caused...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Vector control; Anuran amphibians; Dengue; Malaria.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200334
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Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds Braz. J. Plant Physiol.
Calderon,Leonardo A; Almeida Filho,Humberto A; Teles,Rozeni C. L; Medrano,Francisco J; Bloch Jr,Carlos; Santoro,Marcelo M; Freitas,Sonia M.
Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds. ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM). Circular dichroism analysis revealed that this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors. ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1. The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Inga cylindrica [Vell.] Mart; Leguminosae; Mimosoideae; Protease inhibitor; Protein stability; Trypsin inhibitor.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202010000200001
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