Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides

Autores
Moreno Cordova, Elena N.; Alvarez Armenta, Andres; Garcia Orozco, Karina D.; Arvizu Flores, Aldo A.; Islas Osuna, Maria A.; Robles Zepeda, Ramon E.; Lopez Zavala, Alonso A.; Laino, Aldana; Sotelo Mundo, Rogerio Rafael
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Loxosceles spp. spiders can cause serious public health issues. Chemical control is commonly used, leading to health and environmental problems. Identifying molecular targets and using them with natural compounds can help develop safer and eco-friendlier biopesticides. We studied the ki-netics and predicted structural characteristics of arginine kinase (EC 2.7.3.3) from Loxosceles laeta (LlAK), a key enzyme in the energy metabolism of these organisms. Additionally, we explored (−)-epigallocatechin gallate (EGCG), a green tea flavonoid, as a potential lead compound for the LlAK active site through fluorescence and in silico analysis, such as molecular docking and mo-lecular dynamics (MD) simulation and MM/PBSA analyses. The results indicate that LlAK is a highly efficient enzyme (KmArg 0.14 mM, KmATP 0.98 mM, kcat 93 s−1, kcat/KmArg 630 s−1 mM−1, kcat/ KmATP 94 s−1 mM−1), which correlates with its structure similarity to others AKs (such as Litopenaeus vannamei, Polybetes pythagoricus, and Rhipicephalus sanguineus) and might be related to its important function in the spider’s energetic metabolism. Furthermore, the MD and MM/PBSA analysis suggests that EGCG interacted with LlAK, specifically at ATP/ADP binding site (RMSD <1 nm) and its interaction is energetically favored for its binding stability (−40 to −15 kcal/mol). Moreover, these results are supported by fluorescence quenching analysis (Kd 58.3 μM and Ka 1.71 × 104 M-1). In this context, LlAK is a promising target for the chemical control of L. laeta, and EGCG could be used in combination with conventional pesticides to manage the population of Loxosceles species in urban areas.
Fil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Alvarez Armenta, Andres. Universidad Nacional Autónoma de México; México
Fil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Arvizu Flores, Aldo A.. Universidad de Sonora; México
Fil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Robles Zepeda, Ramon E.. Universidad de Sonora; México
Fil: Lopez Zavala, Alonso A.. Universidad de Sonora; México
Fil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; México
Materia
SPIDER
LOXOSCELES LAETA
GREEN TEA
DOCKING
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/273479
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/273479
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticidesMoreno Cordova, Elena N.Alvarez Armenta, AndresGarcia Orozco, Karina D.Arvizu Flores, Aldo A.Islas Osuna, Maria A.Robles Zepeda, Ramon E.Lopez Zavala, Alonso A.Laino, AldanaSotelo Mundo, Rogerio RafaelSPIDERLOXOSCELES LAETAGREEN TEADOCKINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Loxosceles spp. spiders can cause serious public health issues. Chemical control is commonly used, leading to health and environmental problems. Identifying molecular targets and using them with natural compounds can help develop safer and eco-friendlier biopesticides. We studied the ki-netics and predicted structural characteristics of arginine kinase (EC 2.7.3.3) from Loxosceles laeta (LlAK), a key enzyme in the energy metabolism of these organisms. Additionally, we explored (−)-epigallocatechin gallate (EGCG), a green tea flavonoid, as a potential lead compound for the LlAK active site through fluorescence and in silico analysis, such as molecular docking and mo-lecular dynamics (MD) simulation and MM/PBSA analyses. The results indicate that LlAK is a highly efficient enzyme (KmArg 0.14 mM, KmATP 0.98 mM, kcat 93 s−1, kcat/KmArg 630 s−1 mM−1, kcat/ KmATP 94 s−1 mM−1), which correlates with its structure similarity to others AKs (such as Litopenaeus vannamei, Polybetes pythagoricus, and Rhipicephalus sanguineus) and might be related to its important function in the spider’s energetic metabolism. Furthermore, the MD and MM/PBSA analysis suggests that EGCG interacted with LlAK, specifically at ATP/ADP binding site (RMSD <1 nm) and its interaction is energetically favored for its binding stability (−40 to −15 kcal/mol). Moreover, these results are supported by fluorescence quenching analysis (Kd 58.3 μM and Ka 1.71 × 104 M-1). In this context, LlAK is a promising target for the chemical control of L. laeta, and EGCG could be used in combination with conventional pesticides to manage the population of Loxosceles species in urban areas.Fil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Alvarez Armenta, Andres. Universidad Nacional Autónoma de México; MéxicoFil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Arvizu Flores, Aldo A.. Universidad de Sonora; MéxicoFil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoFil: Robles Zepeda, Ramon E.. Universidad de Sonora; MéxicoFil: Lopez Zavala, Alonso A.. Universidad de Sonora; MéxicoFil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; MéxicoCell Press2024-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/273479Moreno Cordova, Elena N.; Alvarez Armenta, Andres; Garcia Orozco, Karina D.; Arvizu Flores, Aldo A.; Islas Osuna, Maria A.; et al.; Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides; Cell Press; Heliyon; 10; 13; 7-2024; 1-142405-8440CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S2405844024100679info:eu-repo/semantics/altIdentifier/doi/10.1016/j.heliyon.2024.e34036info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:02:34Zoai:ri.conicet.gov.ar:11336/273479instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 12:02:34.845CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
title Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
spellingShingle Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
Moreno Cordova, Elena N.
SPIDER
LOXOSCELES LAETA
GREEN TEA
DOCKING
title_short Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
title_full Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
title_fullStr Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
title_full_unstemmed Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
title_sort Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides
dc.creator.none.fl_str_mv Moreno Cordova, Elena N.
Alvarez Armenta, Andres
Garcia Orozco, Karina D.
Arvizu Flores, Aldo A.
Islas Osuna, Maria A.
Robles Zepeda, Ramon E.
Lopez Zavala, Alonso A.
Laino, Aldana
Sotelo Mundo, Rogerio Rafael
author Moreno Cordova, Elena N.
author_facet Moreno Cordova, Elena N.
Alvarez Armenta, Andres
Garcia Orozco, Karina D.
Arvizu Flores, Aldo A.
Islas Osuna, Maria A.
Robles Zepeda, Ramon E.
Lopez Zavala, Alonso A.
Laino, Aldana
Sotelo Mundo, Rogerio Rafael
author_role author
author2 Alvarez Armenta, Andres
Garcia Orozco, Karina D.
Arvizu Flores, Aldo A.
Islas Osuna, Maria A.
Robles Zepeda, Ramon E.
Lopez Zavala, Alonso A.
Laino, Aldana
Sotelo Mundo, Rogerio Rafael
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv SPIDER
LOXOSCELES LAETA
GREEN TEA
DOCKING
topic SPIDER
LOXOSCELES LAETA
GREEN TEA
DOCKING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Loxosceles spp. spiders can cause serious public health issues. Chemical control is commonly used, leading to health and environmental problems. Identifying molecular targets and using them with natural compounds can help develop safer and eco-friendlier biopesticides. We studied the ki-netics and predicted structural characteristics of arginine kinase (EC 2.7.3.3) from Loxosceles laeta (LlAK), a key enzyme in the energy metabolism of these organisms. Additionally, we explored (−)-epigallocatechin gallate (EGCG), a green tea flavonoid, as a potential lead compound for the LlAK active site through fluorescence and in silico analysis, such as molecular docking and mo-lecular dynamics (MD) simulation and MM/PBSA analyses. The results indicate that LlAK is a highly efficient enzyme (KmArg 0.14 mM, KmATP 0.98 mM, kcat 93 s−1, kcat/KmArg 630 s−1 mM−1, kcat/ KmATP 94 s−1 mM−1), which correlates with its structure similarity to others AKs (such as Litopenaeus vannamei, Polybetes pythagoricus, and Rhipicephalus sanguineus) and might be related to its important function in the spider’s energetic metabolism. Furthermore, the MD and MM/PBSA analysis suggests that EGCG interacted with LlAK, specifically at ATP/ADP binding site (RMSD <1 nm) and its interaction is energetically favored for its binding stability (−40 to −15 kcal/mol). Moreover, these results are supported by fluorescence quenching analysis (Kd 58.3 μM and Ka 1.71 × 104 M-1). In this context, LlAK is a promising target for the chemical control of L. laeta, and EGCG could be used in combination with conventional pesticides to manage the population of Loxosceles species in urban areas.
Fil: Moreno Cordova, Elena N.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Alvarez Armenta, Andres. Universidad Nacional Autónoma de México; México
Fil: Garcia Orozco, Karina D.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Arvizu Flores, Aldo A.. Universidad de Sonora; México
Fil: Islas Osuna, Maria A.. Centro de Investigación E/alimentos y Desarrollo A.c; México
Fil: Robles Zepeda, Ramon E.. Universidad de Sonora; México
Fil: Lopez Zavala, Alonso A.. Universidad de Sonora; México
Fil: Laino, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Sotelo Mundo, Rogerio Rafael. Centro de Investigación E/alimentos y Desarrollo A.c; México
description Loxosceles spp. spiders can cause serious public health issues. Chemical control is commonly used, leading to health and environmental problems. Identifying molecular targets and using them with natural compounds can help develop safer and eco-friendlier biopesticides. We studied the ki-netics and predicted structural characteristics of arginine kinase (EC 2.7.3.3) from Loxosceles laeta (LlAK), a key enzyme in the energy metabolism of these organisms. Additionally, we explored (−)-epigallocatechin gallate (EGCG), a green tea flavonoid, as a potential lead compound for the LlAK active site through fluorescence and in silico analysis, such as molecular docking and mo-lecular dynamics (MD) simulation and MM/PBSA analyses. The results indicate that LlAK is a highly efficient enzyme (KmArg 0.14 mM, KmATP 0.98 mM, kcat 93 s−1, kcat/KmArg 630 s−1 mM−1, kcat/ KmATP 94 s−1 mM−1), which correlates with its structure similarity to others AKs (such as Litopenaeus vannamei, Polybetes pythagoricus, and Rhipicephalus sanguineus) and might be related to its important function in the spider’s energetic metabolism. Furthermore, the MD and MM/PBSA analysis suggests that EGCG interacted with LlAK, specifically at ATP/ADP binding site (RMSD <1 nm) and its interaction is energetically favored for its binding stability (−40 to −15 kcal/mol). Moreover, these results are supported by fluorescence quenching analysis (Kd 58.3 μM and Ka 1.71 × 104 M-1). In this context, LlAK is a promising target for the chemical control of L. laeta, and EGCG could be used in combination with conventional pesticides to manage the population of Loxosceles species in urban areas.
publishDate 2024
dc.date.none.fl_str_mv 2024-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/273479
Moreno Cordova, Elena N.; Alvarez Armenta, Andres; Garcia Orozco, Karina D.; Arvizu Flores, Aldo A.; Islas Osuna, Maria A.; et al.; Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides; Cell Press; Heliyon; 10; 13; 7-2024; 1-14
2405-8440
CONICET Digital
CONICET
url http://hdl.handle.net/11336/273479
identifier_str_mv Moreno Cordova, Elena N.; Alvarez Armenta, Andres; Garcia Orozco, Karina D.; Arvizu Flores, Aldo A.; Islas Osuna, Maria A.; et al.; Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Loxosceles laeta): A potential synergist to chemical pesticides; Cell Press; Heliyon; 10; 13; 7-2024; 1-14
2405-8440
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S2405844024100679
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.heliyon.2024.e34036
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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