Penicillin-binding proteins (PBPs) determine antibiotic action in Langmuir monolayers as nanoarchitectonics mimetic membranes of methicillin-resistant Staphylococcus aureus

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Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorMartins, Beatriz Araújo-
Autor(es): dc.creatorDeffune, Elenice-
Autor(es): dc.creatorOliveira, Osvaldo N.-
Autor(es): dc.creatorMoraes, Marli Leite de-
Data de aceite: dc.date.accessioned2025-08-21T15:56:38Z-
Data de disponibilização: dc.date.available2025-08-21T15:56:38Z-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-05-01-
Data de envio: dc.date.issued2022-06-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2022.112447-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/234287-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/234287-
Descrição: dc.descriptionThe membrane of methicillin-resistant Staphylococcus aureus (MRSA) contains penicillin-binding proteins (PBPs) in the phospholipidic bilayer, with the protein PBP2a being linked with the resistance mechanism. In this work we confirm the role of PBP2a with molecular-level information obtained with Langmuir monolayers as cell membrane models. The MRSA cell membrane was mimicked with a mixed monolayer of dipalmitoyl phosphatidyl glycerol (DPPG) and cardiolipin (CL), also incorporating PBP2a. The surface pressure-area isotherms and the Brewster angle microscopy (BAM) images for these mixed monolayers were significantly affected by the antibiotic meropenem, which is PBP2a inhibitor. The meropenem effects were associated with the presence of PBP2a, as they were absent in the Langmuir monolayers without PBP2a. The relevance of PBP2a was confirmed with results where the antibiotic methicillin, known to be unsuitable to kill MRSA, had the same effects on mixed DPPG/CL and DPPG/CL-PBP2a monolayers since it prevented PBP2a from incorporating in the monolayer. The biological implication of the findings presented here is that a successful antibiotic against MRSA should be able to interact with PBP2a, but in the membrane.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionInstituto Nacional de Ciência e Tecnologia em Eletrônica Orgânica-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionFederal University of São Paulo Institute of Science and Technology, São José dos Campos, SP-
Descrição: dc.descriptionSão Paulo State University Blood Center Botucatu, SP-
Descrição: dc.descriptionSao Carlos Institute of Physics University of Sao Paulo CP 369, SP-
Descrição: dc.descriptionSão Paulo State University Blood Center Botucatu, SP-
Descrição: dc.descriptionFAPESP: 2018/22214-6-
Idioma: dc.languageen-
Relação: dc.relationColloids and Surfaces B: Biointerfaces-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAntibiotic-
Palavras-chave: dc.subjectBrewster angle microscope-
Palavras-chave: dc.subjectLangmuir film-
Palavras-chave: dc.subjectMeropenem-
Palavras-chave: dc.subjectMethicillin-resistant Staphylococcus aureus-
Palavras-chave: dc.subjectModel membrane-
Título: dc.titlePenicillin-binding proteins (PBPs) determine antibiotic action in Langmuir monolayers as nanoarchitectonics mimetic membranes of methicillin-resistant Staphylococcus aureus-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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