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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes

Texto completo
Kumagai, Patricia S. [1] ; Sousa, Victor K. [2] ; Donato, Maressa [2] ; Itri, Rosangela [2] ; Beltramini, Leila M. [1] ; Araujo, Ana P. U. [1] ; Buerck, Jochen [3] ; Wallace, B. A. [4] ; Lopes, Jose L. S. [2]
Número total de Autores: 9
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Inst Fis Sao Carlos, BR-13563120 Sao Carlos, SP - Brazil
[2] Univ Sao Paulo, Inst Fis, Dept Fis Aplicada, Rua Matao 1371, BR-05508090 Sao Paulo, SP - Brazil
[3] Karlsruhe Inst Technol, Inst Biol Interfaces IBG 2, POB 3640, D-76021 Karlsruhe - Germany
[4] Univ London, Birkbeck Coll, Inst Struct & Mol Biol, London WC1E 7HX - England
Número total de Afiliações: 4
Tipo de documento: Artigo Científico
Citações Web of Science: 1

Antimicrobial peptides are a large group of natural compounds which present promising properties for the pharmaceutical and food industries, such as broad-spectrum activity, potential for use as natural preservatives, and reduced propensity for development of bacterial resistance. Plantaricin 149 (Pln149), isolated from Lactobacillus plantarum NRIC 149, is an intrinsically disordered peptide with the ability to inhibit bacteria from the Listeria and Staphylococcus genera, and which is capable of promoting inhibition and disruption of yeast cells. In this study, the interactions of Pln149 with model membranes composed of zwitterionic and/or anionic phospholipids were investigated using a range of biophysical techniques, including isothermal titration calorimetry, surface tension measurements, synchrotron radiation circular dichroism spectroscopy, oriented circular dichroism spectroscopy, and optical microscopy, to elucidate these peptides' mode of interactions and provide insight into their functional roles. In anionic model membranes, the binding of Pln149 to lipid bilayers is an endothermic process and induces a helical secondary structure in the peptide. The helices bind parallel to the surfaces of lipid bilayers and can promote vesicle disruption, depending on peptide concentration. Although Pln149 has relatively low affinity for zwitterionic liposomes, it is able to adsorb at their lipid interfaces, disturbing the lipid packing, assuming a similar parallel helix structure with a surface-bound orientation, and promoting an increase in the membrane surface area. Such findings can explain the intriguing inhibitory action of Pln149 in yeast cells whose cell membranes have a significant zwitterionic lipid composition. (AU)

Processo FAPESP: 15/50347-2 - Estudos biofísicos da estrutura/função de peptídeos antimicrobianos e enzimas isoladas de organismos extremófilos
Beneficiário:Ana Paula Ulian de Araujo
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 13/07600-3 - CIBFar - Centro de Inovação em Biodiversidade e Fármacos
Beneficiário:Glaucius Oliva
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 18/19546-7 - Mecanismos moleculares da ligação, inserção e orientação de peptídeos antimicrobianos em modelos de membrana
Beneficiário:Jose Luiz de Souza Lopes
Linha de fomento: Auxílio à Pesquisa - Regular