Structure and Biological Functions of β-Hairpin Antimicrobial Peptides

Abstract

Antimicrobial peptides (AMPs) are evolutionarily ancient factors of the innate immune system that serve as a crucial first line of defense for humans, animals, and plants against infection. This review focuses on the structural organization, biosynthesis, and biological functions of AMPs that possess a β-hairpin spatial structure. Representatives of this class of AMPs are among the most active antibiotic molecules of animal origin. Due to their wide spectrum of activity and resistance to internal environmental factors, natural β-hairpin AMPbased compounds might become the most promising drug candidates.

Antimicrobial peptides of invertebrates. Part 1. structure, biosynthesis, and evolution

“…Their structure is a double β sheet with its antiparallel chains that are connected by β turn and one (thanatin [52], arenicin 1 and arenicin 2 [36]) or two (tachyples ins [53], polyphemusins [54], androctonin [34], gomesin [22], and NZ17000 [132]) disulfide bonds [133] (nos. 1, 3, 7, 16, and 17; Fig.…”

Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity

“…A high degree of hydrophobicity is often considered to be the main cause of increased toxicity of AMPs. Although a high hydrophobicity level is required for bacterial membrane permeabilization, it leads to binding also to eukaryotic cell membranes as a result M A N U S C R I P T A C C E P T E D ACCEPTED MANUSCRIPT 3 Earlier, we have discovered a new family of 21-residue β-hairpin AMPs, termed arenicins, in coelomocytes of marine polychaeta lugworm Arenicola marina [7]. It was proposed that the peptide dimeric assembly by association of the N-terminal β-strands in membrane-mimicking environment of DPC micelles is retained in the bilayer membranes containing negatively charged lipids, and arenicin antimicrobial activity is mediated by the formation of toroidal pores assembled of several β-structural peptide dimers and lipid molecules [8].…”

“…Among the most active and stable under physiological conditions AMPs are the peptides of animal origin that adopt a β-hairpin conformation stabilized by disulfide bridges [3].…”

Interaction of cationic antimicrobial peptides from Australian frogs with lipid membranes

“…These peptides usually exhibit selective antimicrobial effects under certain conditions and are able to display β‐sheet conformation in aqueous condition. β‐hairpin or loop structures constructed by a single disulfide bond connection, such as lactoferricin B, cyclic peptides, and extended AMPs which are normally linear in shape may contain d ‐ or unnatural amino acids such as aminoisobutyric acid . Some peptides do not fit neatly into a category, for example, indolicidin, which is unstructured in aqueous solution and forms boat‐like conformation in a lipid membrane system; and the defensin‐like AMP, plectasin, that have a mix of α‐helix and antiparallel β‐sheet .…”