Chemical and Biological Characteristics of Antimicrobial α-Helical Peptides Found in Solitary Wasp Venoms and Their Interactions with Model Membranes

Abstract

Solitary wasps use their stinging venoms for paralyzing insect or spider prey and feeding them to their larvae. We have surveyed bioactive substances in solitary wasp venoms, and found antimicrobial peptides together with some other bioactive peptides. Eumenine mastoparan-AF (EMP-AF) was the first to be found from the venom of the solitary eumenine wasp Anterhynchium flavomarginatum micado, showing antimicrobial, histamine-releasing, and hemolytic activities, and adopting an α-helical secondary structure under appropriate conditions. Further survey of solitary wasp venom components revealed that eumenine wasp venoms contained such antimicrobial α-helical peptides as the major peptide component. This review summarizes the results obtained from the studies of these peptides in solitary wasp venoms and some analogs from the viewpoint of (1) chemical and biological characterization; (2) physicochemical properties and secondary structure; and (3) channel-like pore-forming properties.

Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus

“…Neuro-VAL had a lower hydrophobic moment (0.17); this suggests that it probably interacts poorly with cell membranes. [24] To characterize the secondary structures of the peptides we recorded circular dichroism (CD) spectra. The spectra indicated that the peptides were unstructured in water, as expected for linear peptides.…”

Antibacterial Activity and Mechanism of Action of the Wasp Vespa Orientalis Venom Peptides

“…The antimicrobial property of V. orientalis venoms is mostly due to their peptides. Many authors detected the antimicrobial properties of different wasp venoms [22,25] . Isolated AMPs from the V. orientalis venom affected the tested bacterial ultrastructure (Figures 1-3).…”

Strategies towards Targeting Gαi/s Proteins: Scanning of Protein‐Protein Interaction Sites To Overcome Inaccessibility

“…A variety of cationic, amphiphilic substances, including neuropeptides, hormones, venom peptides, and polyamines, exhibited activating properties on purified G proteins. They have a high proportion of hydrophobic and basic groups orienting in an amphipathic α‐helical structure in the presence of phospholipids (Figure 4C), and allowing them to penetrate the cell membrane [134,135] . Prominent members of this group are the wasp venom 14mer peptide mastoparan (H‐INLKALAALAKKIL‐NH 2 ) and the bee venom 26mer peptide melittin (H‐GIGAVLKVLTTGLPALISWIKRKRQQ‐NH 2 ).…”