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Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides

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Abstract

The indiscriminate use of conventional antibiotics is leading to an increase in the number of resistant bacterial strains, motivating the search for new compounds to overcome this challenging problem. Antimicrobial peptides, acting only in the lipid phase of membranes without requiring specific membrane receptors as do conventional antibiotics, have shown great potential as possible substituents of these drugs. These peptides are in general rich in basic and hydrophobic residues forming an amphipathic structure when in contact with membranes. The outer leaflet of the prokaryotic cell membrane is rich in anionic lipids, while the surface of the eukaryotic cell is zwitterionic. Due to their positive net charge, many of these peptides are selective to the prokaryotic membrane. Notwithstanding this preference for anionic membranes, some of them can also act on neutral ones, hampering their therapeutic use. In addition to the electrostatic interaction driving peptide adsorption by the membrane, the ability of the peptide to perturb lipid packing is of paramount importance in their capacity to induce cell lysis, which is strongly dependent on electrostatic and hydrophobic interactions. In the present research, we revised the adsorption of antimicrobial peptides by model membranes as well as the perturbation that they induce in lipid packing. In particular, we focused on some peptides that have simultaneously acidic and basic residues. The net charges of these peptides are modulated by pH changes and the lipid composition of model membranes. We discuss the experimental approaches used to explore these aspects of lipid membranes using lipid vesicles and lipid monolayer as model membranes.

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Acknowledgments

The authors acknowledge financial support from São Paulo Research Foundation - FAPESP (J.R.N. Grants #2015/25619-9 and D.S.A has a post-doctorate fellowship, grants #2015/25620-7). J.R.N. is a researcher for Brazil’s National Council for Scientific and Technological Development (CNPq). T.G.V. has a PhD fellowship from CNPq. DSA thanks UNESP and CAPES for former scholarships. The authors thank Dr. Paul Andrew Beales from the University of Leeds (UK) and Dr. Ernesto E. Ambroggio from the University of Cordoba (Argentina) with whom the FCM experiments were performed in collaborative projects.

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  1. Department of Physics, UNESP - São Paulo State University, IBILCE, R. Cristóvão Colombo, 2265, São José do Rio Preto, SP, CEP 15054-000, Brazil

    Dayane S. Alvares, Taisa Giordano Viegas & João Ruggiero Neto

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  1. Dayane S. Alvares
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  2. Taisa Giordano Viegas
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  3. João Ruggiero Neto
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Correspondence to João Ruggiero Neto.

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Dayane S. Alvares declares that she has no conflicts of interest. Taisa Giordano Viegas declares that she has no conflicts of interest. João Ruggiero Neto declares that he has no conflicts of interest.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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This article is part of a Special Issue on ‘Latin America’ edited by Pietro Ciancaglini and Rosangela Itri

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Alvares, D.S., Viegas, T.G. & Ruggiero Neto, J. Lipid-packing perturbation of model membranes by pH-responsive antimicrobial peptides. Biophys Rev 9, 669–682 (2017). https://doi.org/10.1007/s12551-017-0296-0

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