Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus
Ano de defesa: | 2019 |
---|---|
Autor(a) principal: | |
Orientador(a): | |
Banca de defesa: | , , |
Tipo de documento: | Dissertação |
Tipo de acesso: | Acesso aberto |
Idioma: | por |
Instituição de defesa: |
Universidade Federal do Maranhão
|
Programa de Pós-Graduação: |
PROGRAMA DE PÓS-GRADUAÇÃO EM CIÊNCIAS DA SAÚDE/CCBS
|
Departamento: |
COORDENAÇÃO DO CURSO DE ENGENHARIA QUÍMICA/CCET
|
País: |
Brasil
|
Palavras-chave em Português: | |
Palavras-chave em Inglês: | |
Área do conhecimento CNPq: | |
Link de acesso: | https://tedebc.ufma.br/jspui/handle/tede/3078 |
Resumo: | The tick Rhipicephalus (Boophilus) microplus is the most impacting hematophagous ectoparasite in Brazilian cattle. Their control is generally made with synthetic chemical compounds. However, inadequate handling and indiscriminate use of acaricides has accelerated the selection of ticks resistant to commercially available active ingredients. Terpenes have become a promising alternative to the use of synthetic compounds to control R. microplus, but the mechanism of action of these compounds is still controversial. Inhibition of the enzyme acetylcholinesterase (AChE) is a known mechanism of action of several acaricides. However little has been explored about the action of terpenes in AChEs. The objective of this work was to evaluate the acaricides action of terpenes, as well as their inhibitory potential in AChE, using resistant and sensitive strain of R. microplus. R. microplus larvae were macerated in 100 mM sodium phosphate buffer; pH 7.0; 0.5% v / v triton X-100; containing protease inhibitors. After thirty minutes, the suspension was centrifuged at 15000x g, 4 °C for 30 minutes. The supernatant was called enzyme extract and used as a source of AChE. AChE activity in the enzyme extract was verified as well as the inhibition of said enzyme by terpenes. Additionally, the acaricides action of terpenes on R. microplus larvae was evaluated. Among the terpenes used, p-cymene, thymol, carvacrol and citral presented acaricide activity with LC50 of 1.75, 1.54, 1.41 and 0.38 mg.mL-1 for susceptible strain and LC50 of 1.40. , 1.81, 1.10 and 1.13 mg.mL-1 for the resistant strain, respectively. Thymol and carvacrol inhibited AChE of susceptible strain larvae with IC50 of 0.93 and 0.04 mg.mL-1, respectively. The IC50 exhibited by eucalyptol, carvacrol and thymol for AChE of resistant strain larvae were 0.36, 0.28 and 0.13 mg.mL-1, respectively. This was the first study to investigate the action of terpenes on susceptible and resistant R. microplus AChE. For some terpenes, the positive correlation between acaricide activity and AChE inhibition suggests inhibition of this enzyme as a mechanism of action. This study contributes to the understanding of the mechanism of action of terpenes, supporting subsequent studies on the use of these products as acaricides. |
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SOARES, Alexandra Martins Dos Santos055002787-46http://lattes.cnpq.br/6434212774237352SOARES, Alexandra Martins Dos Santoshttp://lattes.cnpq.br/6434212774237352ROCHA, Cláudia Quintino dahttp://lattes.cnpq.br/5609489233382242TEIXEIRA, Claudener Souzahttp://lattes.cnpq.br/0728801046272432053078003-80http://lattes.cnpq.br/5297318622366268CARDOSO, Alana Dos Santos2020-02-21T16:25:50Z2019-12-06CARDOSO, Alana Dos Santos. Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus. 2019. 57 f. Dissertação (Programa de Pós-Graduação em Ciências da Saúde/CCBS) - Universidade Federal do Maranhão, São Luís, 2019.https://tedebc.ufma.br/jspui/handle/tede/3078ark:/70116/0013000006kgtThe tick Rhipicephalus (Boophilus) microplus is the most impacting hematophagous ectoparasite in Brazilian cattle. Their control is generally made with synthetic chemical compounds. However, inadequate handling and indiscriminate use of acaricides has accelerated the selection of ticks resistant to commercially available active ingredients. Terpenes have become a promising alternative to the use of synthetic compounds to control R. microplus, but the mechanism of action of these compounds is still controversial. Inhibition of the enzyme acetylcholinesterase (AChE) is a known mechanism of action of several acaricides. However little has been explored about the action of terpenes in AChEs. The objective of this work was to evaluate the acaricides action of terpenes, as well as their inhibitory potential in AChE, using resistant and sensitive strain of R. microplus. R. microplus larvae were macerated in 100 mM sodium phosphate buffer; pH 7.0; 0.5% v / v triton X-100; containing protease inhibitors. After thirty minutes, the suspension was centrifuged at 15000x g, 4 °C for 30 minutes. The supernatant was called enzyme extract and used as a source of AChE. AChE activity in the enzyme extract was verified as well as the inhibition of said enzyme by terpenes. Additionally, the acaricides action of terpenes on R. microplus larvae was evaluated. Among the terpenes used, p-cymene, thymol, carvacrol and citral presented acaricide activity with LC50 of 1.75, 1.54, 1.41 and 0.38 mg.mL-1 for susceptible strain and LC50 of 1.40. , 1.81, 1.10 and 1.13 mg.mL-1 for the resistant strain, respectively. Thymol and carvacrol inhibited AChE of susceptible strain larvae with IC50 of 0.93 and 0.04 mg.mL-1, respectively. The IC50 exhibited by eucalyptol, carvacrol and thymol for AChE of resistant strain larvae were 0.36, 0.28 and 0.13 mg.mL-1, respectively. This was the first study to investigate the action of terpenes on susceptible and resistant R. microplus AChE. For some terpenes, the positive correlation between acaricide activity and AChE inhibition suggests inhibition of this enzyme as a mechanism of action. This study contributes to the understanding of the mechanism of action of terpenes, supporting subsequent studies on the use of these products as acaricides.O carrapato Rhipicephalus (Boophilus) microplus é o ectoparasita hematófago de maior impacto na bovinocultura brasileira. Seu controle é, em geral, feito com compostos químicos sintéticos. Entretanto, o manejo inadequado e utilização indiscriminada dos carrapaticidas vêm acelerando a seleção de carrapatos resistentes aos princípios ativos disponíveis comercialmente. Terpenos têm se tornado uma alternativa promissora ao uso de compostos sintéticos para o controle de R. microplus, mas o mecanismo de ação destes compostos ainda é controverso. A inibição da enzima acetilcolinesterase (AChE) é um mecanismo de ação já conhecido de diversos carrapaticidas. Entretanto pouco se tem explorado sobre a ação de terpenos em AChEs. O objetivo deste trabalho foi avaliar a ação carrapaticida de terpenos, assim como seu potencial inibitório em AChE, utilizando-se cepa resistente e sensível de R. microplus. Larvas de R. microplus foram submetidas a maceração em tampão fosfato de sódio 100 mM; pH 7,0; 0,5% v/v de triton X-100; contendo inibidores de proteases. Após trinta minutos, a suspensão foi centrifugada à 15000 x g, 4 ºC, por 30 minutos. O sobrenadante foi denominado extrato enzimático e usado como fonte de AChE. Verificou-se a atividade AChE no extrato enzimático assim como a inibição da referida enzima por terpenos. Adicionalmente, avaliou-se a ação carrapaticida de terpenos sobre larvas de R. microplus. Entre os terpenos utilizados o p-cimeno, timol, carvacrol e citral apresentaram atividade carrapaticida com CL50 de 1,75, 1,54, 1,41 e 0,38 mg.mL-1 para a cepa suscetível e CL50 de 1,40, 1,81, 1,10 e 1,13 mg.mL-1 para a cepa resistente, respectivamente. O timol e o carvacrol inibiram a AChE das larvas de cepa suscetíveis com IC50 de 0,93 e 0,04 mg.mL-1, respectivamente. A IC50 exibida por eucaliptol, carvacrol e timol para AChE das larvas de linhagens resistentes foi de 0,36, 0,28 e 0,13 mg.mL-1, respectivamente. Este foi o primeiro estudo a investigar a ação dos terpenos na AChE de R. microplus suscetível e resistente. Para alguns terpenos, a correlação positiva entre atividade carrapaticida e inibição da AChE sugere a inibição desta enzima como mecanismo de ação. Esse estudo contribui com o entendimento do mecanismo de ação de terpenos, dando suporte para estudos subsequentes sobre o uso destes produtos como carrapaticidas.Submitted by Sheila MONTEIRO (sheila.monteiro@ufma.br) on 2020-02-21T16:25:50Z No. of bitstreams: 1 ALANA-CARDOSO.pdf: 1612941 bytes, checksum: ce2a46e9f9d6306823f3d502475a28e7 (MD5)Made available in DSpace on 2020-02-21T16:25:50Z (GMT). No. of bitstreams: 1 ALANA-CARDOSO.pdf: 1612941 bytes, checksum: ce2a46e9f9d6306823f3d502475a28e7 (MD5) Previous issue date: 2019-12-06Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - CAPESapplication/pdfporUniversidade Federal do MaranhãoPROGRAMA DE PÓS-GRADUAÇÃO EM CIÊNCIAS DA SAÚDE/CCBSUFMABrasilCOORDENAÇÃO DO CURSO DE ENGENHARIA QUÍMICA/CCETRhipicephalus microplusAcetilcolinesteraseTerpenosRhipicephalus microplusAcetylcholinesteraseTerpenesCiências da SaúdeAtividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplusAcaricidal activity and inhibition of acetylcholinesterase by terpenes in Rhipicephalus (Boophilus) microplusinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisinfo:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UFMAinstname:Universidade Federal do Maranhão (UFMA)instacron:UFMAORIGINALALANA-CARDOSO.pdfALANA-CARDOSO.pdfapplication/pdf1612941http://tedebc.ufma.br:8080/bitstream/tede/3078/2/ALANA-CARDOSO.pdfce2a46e9f9d6306823f3d502475a28e7MD52LICENSElicense.txtlicense.txttext/plain; charset=utf-82255http://tedebc.ufma.br:8080/bitstream/tede/3078/1/license.txt97eeade1fce43278e63fe063657f8083MD51tede/30782020-02-21 13:25:50.086oai:tede2: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Biblioteca Digital de Teses e Dissertaçõeshttps://tedebc.ufma.br/jspui/PUBhttp://tedebc.ufma.br:8080/oai/requestrepositorio@ufma.br||repositorio@ufma.bropendoar:21312020-02-21T16:25:50Biblioteca Digital de Teses e Dissertações da UFMA - Universidade Federal do Maranhão (UFMA)false |
dc.title.por.fl_str_mv |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
dc.title.alternative.eng.fl_str_mv |
Acaricidal activity and inhibition of acetylcholinesterase by terpenes in Rhipicephalus (Boophilus) microplus |
title |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
spellingShingle |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus CARDOSO, Alana Dos Santos Rhipicephalus microplus Acetilcolinesterase Terpenos Rhipicephalus microplus Acetylcholinesterase Terpenes Ciências da Saúde |
title_short |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
title_full |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
title_fullStr |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
title_full_unstemmed |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
title_sort |
Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus |
author |
CARDOSO, Alana Dos Santos |
author_facet |
CARDOSO, Alana Dos Santos |
author_role |
author |
dc.contributor.advisor1.fl_str_mv |
SOARES, Alexandra Martins Dos Santos |
dc.contributor.advisor1ID.fl_str_mv |
055002787-46 |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/6434212774237352 |
dc.contributor.referee1.fl_str_mv |
SOARES, Alexandra Martins Dos Santos |
dc.contributor.referee1Lattes.fl_str_mv |
http://lattes.cnpq.br/6434212774237352 |
dc.contributor.referee2.fl_str_mv |
ROCHA, Cláudia Quintino da |
dc.contributor.referee2Lattes.fl_str_mv |
http://lattes.cnpq.br/5609489233382242 |
dc.contributor.referee3.fl_str_mv |
TEIXEIRA, Claudener Souza |
dc.contributor.referee3Lattes.fl_str_mv |
http://lattes.cnpq.br/0728801046272432 |
dc.contributor.authorID.fl_str_mv |
053078003-80 |
dc.contributor.authorLattes.fl_str_mv |
http://lattes.cnpq.br/5297318622366268 |
dc.contributor.author.fl_str_mv |
CARDOSO, Alana Dos Santos |
contributor_str_mv |
SOARES, Alexandra Martins Dos Santos SOARES, Alexandra Martins Dos Santos ROCHA, Cláudia Quintino da TEIXEIRA, Claudener Souza |
dc.subject.por.fl_str_mv |
Rhipicephalus microplus Acetilcolinesterase Terpenos |
topic |
Rhipicephalus microplus Acetilcolinesterase Terpenos Rhipicephalus microplus Acetylcholinesterase Terpenes Ciências da Saúde |
dc.subject.eng.fl_str_mv |
Rhipicephalus microplus Acetylcholinesterase Terpenes |
dc.subject.cnpq.fl_str_mv |
Ciências da Saúde |
description |
The tick Rhipicephalus (Boophilus) microplus is the most impacting hematophagous ectoparasite in Brazilian cattle. Their control is generally made with synthetic chemical compounds. However, inadequate handling and indiscriminate use of acaricides has accelerated the selection of ticks resistant to commercially available active ingredients. Terpenes have become a promising alternative to the use of synthetic compounds to control R. microplus, but the mechanism of action of these compounds is still controversial. Inhibition of the enzyme acetylcholinesterase (AChE) is a known mechanism of action of several acaricides. However little has been explored about the action of terpenes in AChEs. The objective of this work was to evaluate the acaricides action of terpenes, as well as their inhibitory potential in AChE, using resistant and sensitive strain of R. microplus. R. microplus larvae were macerated in 100 mM sodium phosphate buffer; pH 7.0; 0.5% v / v triton X-100; containing protease inhibitors. After thirty minutes, the suspension was centrifuged at 15000x g, 4 °C for 30 minutes. The supernatant was called enzyme extract and used as a source of AChE. AChE activity in the enzyme extract was verified as well as the inhibition of said enzyme by terpenes. Additionally, the acaricides action of terpenes on R. microplus larvae was evaluated. Among the terpenes used, p-cymene, thymol, carvacrol and citral presented acaricide activity with LC50 of 1.75, 1.54, 1.41 and 0.38 mg.mL-1 for susceptible strain and LC50 of 1.40. , 1.81, 1.10 and 1.13 mg.mL-1 for the resistant strain, respectively. Thymol and carvacrol inhibited AChE of susceptible strain larvae with IC50 of 0.93 and 0.04 mg.mL-1, respectively. The IC50 exhibited by eucalyptol, carvacrol and thymol for AChE of resistant strain larvae were 0.36, 0.28 and 0.13 mg.mL-1, respectively. This was the first study to investigate the action of terpenes on susceptible and resistant R. microplus AChE. For some terpenes, the positive correlation between acaricide activity and AChE inhibition suggests inhibition of this enzyme as a mechanism of action. This study contributes to the understanding of the mechanism of action of terpenes, supporting subsequent studies on the use of these products as acaricides. |
publishDate |
2019 |
dc.date.issued.fl_str_mv |
2019-12-06 |
dc.date.accessioned.fl_str_mv |
2020-02-21T16:25:50Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
CARDOSO, Alana Dos Santos. Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus. 2019. 57 f. Dissertação (Programa de Pós-Graduação em Ciências da Saúde/CCBS) - Universidade Federal do Maranhão, São Luís, 2019. |
dc.identifier.uri.fl_str_mv |
https://tedebc.ufma.br/jspui/handle/tede/3078 |
dc.identifier.dark.fl_str_mv |
ark:/70116/0013000006kgt |
identifier_str_mv |
CARDOSO, Alana Dos Santos. Atividade acaricida e inibição da acetilcolinesterase por terpenos em Rhipicephalus (Boophilus) microplus. 2019. 57 f. Dissertação (Programa de Pós-Graduação em Ciências da Saúde/CCBS) - Universidade Federal do Maranhão, São Luís, 2019. ark:/70116/0013000006kgt |
url |
https://tedebc.ufma.br/jspui/handle/tede/3078 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Federal do Maranhão |
dc.publisher.program.fl_str_mv |
PROGRAMA DE PÓS-GRADUAÇÃO EM CIÊNCIAS DA SAÚDE/CCBS |
dc.publisher.initials.fl_str_mv |
UFMA |
dc.publisher.country.fl_str_mv |
Brasil |
dc.publisher.department.fl_str_mv |
COORDENAÇÃO DO CURSO DE ENGENHARIA QUÍMICA/CCET |
publisher.none.fl_str_mv |
Universidade Federal do Maranhão |
dc.source.none.fl_str_mv |
reponame:Biblioteca Digital de Teses e Dissertações da UFMA instname:Universidade Federal do Maranhão (UFMA) instacron:UFMA |
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UFMA |
institution |
UFMA |
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Biblioteca Digital de Teses e Dissertações da UFMA |
collection |
Biblioteca Digital de Teses e Dissertações da UFMA |
bitstream.url.fl_str_mv |
http://tedebc.ufma.br:8080/bitstream/tede/3078/2/ALANA-CARDOSO.pdf http://tedebc.ufma.br:8080/bitstream/tede/3078/1/license.txt |
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Biblioteca Digital de Teses e Dissertações da UFMA - Universidade Federal do Maranhão (UFMA) |
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repositorio@ufma.br||repositorio@ufma.br |
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