The interaction of antimicrobial peptides with membranes

• Published in: Advances in colloid and interface science Vol. 247; pp. 521 - 532
• Main Authors: Travkova, Oksana G., Moehwald, Helmuth, Brezesinski, Gerald
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.09.2017
• Subjects: Animals; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - metabolism; Antimicrobial peptides; Arenicin; Helminth Proteins - chemistry; Helminth Proteins - metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; IRRAS; Lipid Bilayers - chemistry; Lipid Bilayers - metabolism; Lipopolysaccharides - chemistry; Lipopolysaccharides - metabolism; Peptides, Cyclic - chemistry; Peptides, Cyclic - metabolism; Phospholipids; Phospholipids - chemistry; Phospholipids - metabolism; Polychaeta - chemistry; Protein Conformation; Specular X-ray reflectivity; Static Electricity; Surface-Active Agents - chemistry; Surface-Active Agents - metabolism; IRRAS; Cd; Specular X-ray reflectivity; Arenicin; Phospholipids; Antimicrobial peptides
• ISSN: 0001-8686; 1873-3727; 1873-3727
• DOI: 10.1016/j.cis.2017.06.001

The interaction of antimicrobial peptides (AMPs) with biological membranes is in the focus of research since several years, and the most important features and modes of action of AMPs are described in this review. Different model systems can be used to understand such interactions on a molecular level. As a special example, we use 2D and 3D model membranes to investigate the interaction of the natural cyclic (Ar-1) and the synthetic linear molecule arenicin with selected amphiphiles and phospholipids. A panoply of sophisticated methods has been used to analyze these interactions on a molecular level. As a general trend, one observes that cationic antimicrobial peptides do not interact with cationic amphiphiles due to electrostatic repulsion, whereas with non-ionic amphiphiles, the peptide interacts only with aggregated systems and not with monomers. The interaction is weak (hydrophobic interaction) and requires an aggregated state with a large surface (cylindrical micelles). Anionic amphiphiles (as monomers or micelles) exhibit strong electrostatic interactions with the AMPs leading to changes in the peptide conformation. Both types of peptides interact strongly with anionic phospholipid monolayers with a preference for fluid layers. The interaction with a zwitterionic layer is almost absent for the linear derivative but measurable for the cyclic arenicin Ar-1. This is in accordance with biological experiments showing that Ar-1 forms well defined stable pores in phospholipid and lipopolysaccharide (LPS) membranes (cytotoxicity). The synthetic linear arenicin, which is less cytotoxic, does not affect the mammalian lipids to such an extent. The interaction of arenicin with bacterial membrane lipids is dominated by hydrogen bonding together with electrostatic and hydrophobic interactions. [Display omitted] •Understanding the interactions of antimicrobial peptides (AMPs) with biological membranes is extremely important.•The most important features and modes of action of AMPs are described.•Different model systems (2D and 3D) are used and described.•Sophisticated methods as IRRAS, BAM, and XR are used and described for monolayers.•The behavior of cyclic arenicin and its linear derivative are described as special examples.