Autor(es): Martins, Beatriz Araújo ; Deffune, Elenice [UNESP] ; Oliveira, Osvaldo N. ; Moraes, Marli Leite de
Data: 2022
Identificador Persistente: http://hdl.handle.net/11449/234287
Origem: Oasisbr
Assunto(s): Antibiotic; Brewster angle microscope; Langmuir film; Meropenem; Methicillin-resistant Staphylococcus aureus; Model membrane
Made available in DSpace on 2022-05-01T15:46:14Z (GMT). No. of bitstreams: 0 Previous issue date: 2022-06-01
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Instituto Nacional de Ciência e Tecnologia em Eletrônica Orgânica
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
The 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.
Federal University of São Paulo Institute of Science and Technology, São José dos Campos, SP
São Paulo State University Blood Center Botucatu, SP
Sao Carlos Institute of Physics University of Sao Paulo CP 369, SP
São Paulo State University Blood Center Botucatu, SP
FAPESP: 2018/22214-6
