Unwrapping the structural and functional features of antimicrobial peptides from wasp venoms

Abstract

The study of wasp venoms has captured attention due to the presence of a wide variety of active compounds, revealing a diverse array of biological effects. Among these compounds, certain antimicrobial peptides (AMPs) such as mastoparans and chemotactic peptides have emerged as significant players, characterized by their unique amphipathic short linear alpha-helical structure. These peptides exhibit not only antibiotic properties but also a range of other biological activities, which are related to their ability to interact with biological membranes to varying degrees. This review article aims to provide updated insights into the structure/function relationships of AMPs derived from wasp venoms, linking this knowledge to the potential development of innovative treatments against infections.

Keywords: Antimicrobial; Hemolytic; Mastoparan A (PubChem CID: 86289586); Mastoparan AF (PubChem CID: 86289585); Mastoparan B (PubChem CID: 86289587); Mastoparan C (PubChem CID: 5487900); Mastoparan D (PubChem CID: 86289588); Mastoparan L (PubChem CID: 6324633); Mastoparan M (PubChem CID: 86289589); Peptide features; Polistes- mastoparan-R1 (PubChem CID: 102146288); Polistes-protonectin (PubChem CID: 102146288); Some chemical compounds studied in this article Mastoparan X (PubChem CID: 86289590); Structure/function; Wasp venoms.