Effects of proteinase inhibitor from Adenanthera pavonina seeds on short- and long term larval development of Aedes aegypti

Sasaki, Daniele Yumi; Jacobowski, Ana Cristina; Souza, Antônio Pancrácio de; Cardoso, Marlon Henrique; Franco, Octávio L.; Macedo, Maria Lígia Rodrigues

doi:10.1016/j.biochi.2015.03.011

Cited by 24 publications

(29 citation statements)

References 65 publications

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“…In our study, we observed all these deleterious effects. Similarly, Sasaki et al . reported that the incubation of Ae.…”

Section: Resultsmentioning

confidence: 85%

“…One of the strategies to eliminate this mosquito is the use of synthetic insecticides belonging to the classes organochlorines, organophosphates and pyrethroids, which generally act on the nervous systems of insects . Although effective, the inadequate management of these insecticides led to the emergence of resistant insect populations, and as a consequence of increased resistance of pests to chemical insecticides, research on natural and biodegradable insecticides that promote larval mortality and avoid the emergence of resistant strains has increased …”

Section: Introductionmentioning

confidence: 99%

“…10 Although effective, the inadequate management of these insecticides led to the emergence of resistant insect populations, and as a consequence of increased resistance of pests to chemical insecticides, research on natural and biodegradable insecticides that promote larval mortality and avoid the emergence of resistant strains has increased. 11,12 Bioinsecticides are ecofriendly pesticides (low toxicity to the environment) which do not cause problems in terms of air and water quality, often targeting only specific insects without having negative effects on non-target insects. They can be used in the management of pests harmful to plants and also to combat vectors of diseases.…”

Section: Introductionmentioning

confidence: 99%

“…For insect population control, the digestive enzymes of the insects have become a potential target of protease inhibitors. 20 The insecticidal potential of protease inhibitors against different insect classes has been reported; for example, protease inhibitors from Adenanthera pavonina (ApTI) 11 , Cassia leiandra (ClTI) 21 and Leucaena leucocephala (LTI) 22 have been reported to have effects on larvae of Ae. aegypti (Diptera), those from Inga vera (IVTI) 23 and Poincianella pyramidalis (PpyTI) 24 have been reported to have effects on Anagasta kuehniella neonates, and a protease inhibitor from Dimorphandra mollis (DMTI-II) 25 has been reported to have effects on Callosobruchus maculatus (Coleoptera).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

Filho

Tabosa

Hissa

et al. 2018

Pest Management Science

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“…In our study, we observed all these deleterious effects. Similarly, Sasaki et al . reported that the incubation of Ae.…”

Section: Resultsmentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

Filho

Tabosa

Hissa

et al. 2018

Pest Management Science

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“…Namely, PdKI, a trypsin inhibitor purifi ed from Pithecelobium dumosum seeds and effective against papain and insect digestive proteinase (Oliveira et al 2007); PTPKI, purifi ed from Prosopis juliflora seeds, shown dual activities for papain and trypsin enzymes (Franco et al 2002). Another inhibitor (ApTI) purifi ed from Adenanthera pavonina seeds inhibited papain, trypsin and chymotrypsin and had a deleterious effect on Callosobruchus maculatus and Aedes aegypti larvae (Macedo et al 2004, Sasaki et al 2015.…”

Section: Discussionmentioning

confidence: 99%

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Brito

Melo

Alves

et al. 2016

Hoehnea

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-(Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions). The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds. Keywords: antimicrobial, cystatin, Fabaceae, protease RESUMO -(Purificação parcial de um inibidor de tripsina/papaína de sementes de Hymenaea courbaril L. e atividade antibacteriana de suas frações proteicas). O extrato bruto e frações proteicas de sementes de Hymenaea courbaril foram investigados para a presença de inibidores de tripsina e papaína e atividade antimicrobiana contra Vibrio parahaemolyticus, Staphylococcus aureus e Escherichia coli. As frações foram obtidas após precipitação do extrato bruto com sulfato de amônio em três faixas de saturação (0-30%, 30-60% e 60-90%) e denominadas Hc030, Hc3060 e Hc6090, respectivamente. O extrato bruto e as frações apresentaram diferente especificidade em inibir a atividade da tripsina e papaína. A atividade antimicrobiana foi observada nas frações Hc030 e Hc3060 e somente contra V. parahaemolyticus. O inibidor isolado a partir de Hc3060 foi mais eficiente na inibição da tripsina (100% de inibição) do que da papaína (54% de inibição), e mostrou uma massa molecular aparente de 20 kDa. Este estudo mostra que as sementes de H. courbaril possuem inibidores de proteases e proteínas com atividade antibacteriana, indicando que a espécie é uma fonte de compostos bioativos.

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Noncompetitive tight‐binding inhibition ofAnticarsia gemmatalistrypsins byAdenanthera pavoninaprotease inhibitor affects larvae survival

Meriño‐Cabrera

Mendes

Castro

et al. 2020

Arch Insect Biochem Physiol

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The economic loss in soybean crops caused by the Lepidoptera insects has encouraged the search for new strategies to control this pest, which are currently based on synthetic insecticides. This paper evaluated the ability of ApTI (Adenanthera pavonina trypsin inhibitor) to inhibit trypsin-like proteins from Anticarsia gemmatalis by docking, molecular dynamics, and enzymatic and survival assay. The docking and molecular dynamic simulation between trypsin and ApTI were performed using the program CLUSPRO and NAMD, respectively. The inhibitory constant K i and the inhibition type were determined through chromogenic assays. The survival assay of neonatal larvae under treatment with artificial diet supplemented with ApTI was also performed. The ApTI binding site was predicted to block substrate access to trypsin due to four interactions with the enzyme, producing a complex with a surface area of 1,183.7 Å 2 .The kinetic analysis revealed a noncompetitive tightbinding mechanism. The survival curves obtained using Kaplan-Meier estimators indicated that the highest larvae mortality was 60%, using 1.2 mg of ApTI per 100 ml of artificial diet. The in vitro, in vivo, and in silico studies demonstrated that ApTI is a strong noncompetitive inhibitor of trypsin with biotechnological potential for the control of A. gemmatalis insect. K E Y W O R D S binding, insects, Kunitz inhibitor, molecular docking, noncompetitive, trypsin enzyme

show abstract

Effects of proteinase inhibitor from Adenanthera pavonina seeds on short- and long term larval development of Aedes aegypti

Cited by 24 publications

References 65 publications

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

First insights into insecticidal activity against Aedes aegypti and partial biochemical characterization of a novel low molecular mass chymotrypsin‐trypsin inhibitor purified from Lonchocarpus sericeus seeds

Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Noncompetitive tight‐binding inhibition ofAnticarsia gemmatalistrypsins byAdenanthera pavoninaprotease inhibitor affects larvae survival

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