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

Author(s)

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]

Affiliation

^[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

• Document type: Journal article
• Source: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS; v. 48, n. 7, p. 621-633, OCT 2019.
• Web of Science Citations: 2

Abstract

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)

• FAPESP's process: 18/19546-7 - Molecular mechanisms of the binding, insertion, and orientation of antimicrobial peptides in model membranes
• Grantee: Jose Luiz de Souza Lopes
• Support Opportunities: Regular Research Grants
• FAPESP's process: 13/07600-3 - CIBFar - Center for Innovation in Biodiversity and Drug Discovery
• Grantee: Glaucius Oliva
• Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC
• FAPESP's process: 15/50347-2 - Biophysical studies of the structure/function of antimicrobial peptides and enzymes isolated from extremophile organisms
• Grantee: Ana Paula Ulian de Araujo
• Support Opportunities: Regular Research Grants