Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers

Detalhes bibliográficos
Autor(a) principal: Moreira, Lucas G. [UNESP]
Data de Publicação: 2021
Outros Autores: Almeida, Alexandre M. [UNESP], Nield, Tyler [UNESP], Camacho, Sabrina A. [UNESP], Aoki, Pedro H.B. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.jphotobiol.2021.112173
http://hdl.handle.net/11449/206121
Resumo: Photodynamic damage to the cell envelope can inactivate microorganisms and may be applied to combat super-resistance phenomenon, empowered by the indiscriminate use of antibiotics. Efficiency in microbial inactivation is dependent on the incorporation of photosensitizers (PS) into the bacterial membranes to trigger oxidation reactions under illumination. Herein, Langmuir monolayers of Escherichia coli lipid extract were built to determine the binding mechanisms and oxidation outcomes induced by eosin decyl ester (EosDEC) and toluidine blue-O (TBO) PSs. Surface-pressure isotherms of the E. coli monolayers were expanded upon EosDEC and TBO, suggesting incorporation of both PSs. Fourier-transform infrared spectroscopy (FTIR) of Langmuir-Schaefer (LS) films reveled that the EosDEC and TBO binding mechanisms are dominated by electrostatic interactions with the anionic polar groups, with limited penetration into the chains. Light-irradiation reduced the relative area of E. coli monolayer on TBO, indicating an increased loss of material to the subphase owing to the chain cleavage, generated by contact-dependent reactions with excited states of TBO. In contrast, the increased relative area of E. coli monolayers containing EosDEC suggests lipid hydroperoxidation, which is PS contact-independent. Even considering a small chain penetration, the saturated EosDEC may have partitioned towards saturated reach domains, avoiding direct contact with membrane unsaturations.
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spelling Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizersPhotodynamic damage to the cell envelope can inactivate microorganisms and may be applied to combat super-resistance phenomenon, empowered by the indiscriminate use of antibiotics. Efficiency in microbial inactivation is dependent on the incorporation of photosensitizers (PS) into the bacterial membranes to trigger oxidation reactions under illumination. Herein, Langmuir monolayers of Escherichia coli lipid extract were built to determine the binding mechanisms and oxidation outcomes induced by eosin decyl ester (EosDEC) and toluidine blue-O (TBO) PSs. Surface-pressure isotherms of the E. coli monolayers were expanded upon EosDEC and TBO, suggesting incorporation of both PSs. Fourier-transform infrared spectroscopy (FTIR) of Langmuir-Schaefer (LS) films reveled that the EosDEC and TBO binding mechanisms are dominated by electrostatic interactions with the anionic polar groups, with limited penetration into the chains. Light-irradiation reduced the relative area of E. coli monolayer on TBO, indicating an increased loss of material to the subphase owing to the chain cleavage, generated by contact-dependent reactions with excited states of TBO. In contrast, the increased relative area of E. coli monolayers containing EosDEC suggests lipid hydroperoxidation, which is PS contact-independent. Even considering a small chain penetration, the saturated EosDEC may have partitioned towards saturated reach domains, avoiding direct contact with membrane unsaturations.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Saõ Paulo State University (UNESP) School of Sciences Humanities and LanguagesFaculty of Engineering University of VictoriaIFSC São Carlos Institute of Physics University of São Paulo (USP)Saõ Paulo State University (UNESP) School of Sciences Humanities and LanguagesFAPESP: 2018/14692-5FAPESP: 2018/16713-0FAPESP: 2018/22214-6FAPESP: 2020/15854-9FAPESP: FAPESP 2013/14262-7Universidade Estadual Paulista (Unesp)University of VictoriaUniversidade de São Paulo (USP)Moreira, Lucas G. [UNESP]Almeida, Alexandre M. [UNESP]Nield, Tyler [UNESP]Camacho, Sabrina A. [UNESP]Aoki, Pedro H.B. [UNESP]2021-06-25T10:26:54Z2021-06-25T10:26:54Z2021-05-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.jphotobiol.2021.112173Journal of Photochemistry and Photobiology B: Biology, v. 218.1873-26821011-1344http://hdl.handle.net/11449/20612110.1016/j.jphotobiol.2021.1121732-s2.0-85103408484Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Photochemistry and Photobiology B: Biologyinfo:eu-repo/semantics/openAccess2021-10-22T21:03:09Zoai:repositorio.unesp.br:11449/206121Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:24:55.393588Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
title Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
spellingShingle Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
Moreira, Lucas G. [UNESP]
title_short Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
title_full Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
title_fullStr Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
title_full_unstemmed Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
title_sort Modulating photochemical reactions in Langmuir monolayers of Escherichia coli lipid extract with the binding mechanisms of eosin decyl ester and toluidine blue-O photosensitizers
author Moreira, Lucas G. [UNESP]
author_facet Moreira, Lucas G. [UNESP]
Almeida, Alexandre M. [UNESP]
Nield, Tyler [UNESP]
Camacho, Sabrina A. [UNESP]
Aoki, Pedro H.B. [UNESP]
author_role author
author2 Almeida, Alexandre M. [UNESP]
Nield, Tyler [UNESP]
Camacho, Sabrina A. [UNESP]
Aoki, Pedro H.B. [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
University of Victoria
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Moreira, Lucas G. [UNESP]
Almeida, Alexandre M. [UNESP]
Nield, Tyler [UNESP]
Camacho, Sabrina A. [UNESP]
Aoki, Pedro H.B. [UNESP]
description Photodynamic damage to the cell envelope can inactivate microorganisms and may be applied to combat super-resistance phenomenon, empowered by the indiscriminate use of antibiotics. Efficiency in microbial inactivation is dependent on the incorporation of photosensitizers (PS) into the bacterial membranes to trigger oxidation reactions under illumination. Herein, Langmuir monolayers of Escherichia coli lipid extract were built to determine the binding mechanisms and oxidation outcomes induced by eosin decyl ester (EosDEC) and toluidine blue-O (TBO) PSs. Surface-pressure isotherms of the E. coli monolayers were expanded upon EosDEC and TBO, suggesting incorporation of both PSs. Fourier-transform infrared spectroscopy (FTIR) of Langmuir-Schaefer (LS) films reveled that the EosDEC and TBO binding mechanisms are dominated by electrostatic interactions with the anionic polar groups, with limited penetration into the chains. Light-irradiation reduced the relative area of E. coli monolayer on TBO, indicating an increased loss of material to the subphase owing to the chain cleavage, generated by contact-dependent reactions with excited states of TBO. In contrast, the increased relative area of E. coli monolayers containing EosDEC suggests lipid hydroperoxidation, which is PS contact-independent. Even considering a small chain penetration, the saturated EosDEC may have partitioned towards saturated reach domains, avoiding direct contact with membrane unsaturations.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-25T10:26:54Z
2021-06-25T10:26:54Z
2021-05-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.jphotobiol.2021.112173
Journal of Photochemistry and Photobiology B: Biology, v. 218.
1873-2682
1011-1344
http://hdl.handle.net/11449/206121
10.1016/j.jphotobiol.2021.112173
2-s2.0-85103408484
url http://dx.doi.org/10.1016/j.jphotobiol.2021.112173
http://hdl.handle.net/11449/206121
identifier_str_mv Journal of Photochemistry and Photobiology B: Biology, v. 218.
1873-2682
1011-1344
10.1016/j.jphotobiol.2021.112173
2-s2.0-85103408484
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Photochemistry and Photobiology B: Biology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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