A Review of the Mechanism of Action of Amphibian Antimicrobial Peptides Focusing on Peptide-Membrane Interaction and Membrane Curvature

Abstract

Research interests on amphibian antimicrobial peptides (AMPs) are currently increasing because of their capability to combat microorganisms from both terrestrial and aquatic environments, which are the warehouses of human pathogens. The most remarkable feature of AMPs are their mechanism of action, primarily targeted to anionic membranes. Researchers have postulated many models to describe peptide- membrane interaction, which leads to membrane permeation/intracellular targeting. Despite these models information regarding the relationship between membrane curvature and peptidemembrane interaction is scarce. This relationship could be clearly depicted using the two-state model and interfacial activity model. In the review, we discuss in detail the two state and interfacial activity models and explain the influence of membrane curvature on peptide binding and the membrane interaction of curvature-sensitive peptides. In addition, the models proposed to explain the mechanism of action of membrane lytic and non-lytic AMPs are also reviewed.

Antimicrobial and Anti-inflammatory Effects of a Novel Peptide From the Skin of Frog Microhyla pulchra

“…The attraction and attachment of AMPs to microbial cell surfaces are crucial to exert their antimicrobial activity ( Vineeth and Sanil, 2017 ). Flow cytometry experiments were implemented to explore the binding of brevinin-2MP to bacteria.…”

High-Throughput Identification of Antimicrobial Peptides from Amphibious Mudskippers

“…As the best candidates to replace antibiotics, AMPs have a bright future for applications in our daily life, especially those from marine resources [ 10 , 11 , 12 , 13 ]. However, their action mechanisms and phylogenetic status are still ambiguous [ 14 , 15 , 16 ].…”

Challenge in the Discovery of New Drugs: Antimicrobial Peptides against WHO-List of Critical and High-Priority Bacteria

“…A cationic net charge along the structure is often observed, which can induce and facilitate an initial interaction with membrane headgroup components. There is also a predominance of hydrophobic residues, up to 50% of the entire sequence, allowing van der Waals interactions with the membrane lipid tails [ 9 , 10 ]. AMPs can adopt a broad variety of secondary structures: the helical magainin; the protegrin, which forms a β-hairpin due to the presence of a disulfide bond; the disordered indolicidin; and gramicidin, which can be cyclic [ 11 ].…”

“…Regarding the nonmembrane lytic peptide mechanism of action, AMPs mostly target intracellular structures, binding to DNA gyrase and topoisomerase IV, directly affecting transcription/replication. In addition, AMPs can inhibit protein and cell wall biosynthesis, inactivate enzyme activities in ribosomes, and cause cellular apoptosis [ 9 , 11 , 13 ].…”