1.C.32 The Amphipathic Peptide Mastoparan (Mastoparan) Family
Mastoparans are 14 (sometimes 13 or 15) amino acyl residue, amphipathic, α-helical peptides present in the venom of hornets, wasps and yellow jackets. They exert numerous biological effects including (1) degranulation of mast cells, (2) G-protein receptor mimicry, (3) phospholipase A2 stimulation, and (4) inhibition of Golgi vesicle transport. They all increase bilayer permeability to hydrophilic solutes by forming short lived pores. Because they are too short to span the membrane as amphipathic α-helices (a configuration they assume when in association with membranes), it is thought that they form bundles of peptides in a so called 'barrel-stove' configuration. Pore formation has been demonstrated electrophysiologically as well as by demonstrating increased permeability to hydrophilic molecules and dyes. They also exhibit cytotoxicity, but certain amino acid substitutions reduce the activity (Irazazabal et al. 2016). Their actual transmembrane architecture is unknown.
The generalized transport reaction catalyzed by mastoparan pores is:
Small molecules (in) Small molecules (out)
Mastoparan (INWKKMAATALKMI). Amiino acid substitutions gave rise to mastoparans that displayed a broad-spectrum antimicrobial activity against bacteria and fungi (MIC in the range 3-25μM), without being hemolytic or cytotoxic (Irazazabal et al. 2016).
Wasps, hornets, yellowjackets
Mastoparan of Parapolybia indica
Mastoparan C (LNLKALLAVAKKIL)
Mastoparan C of Vespa crabro
Polistes Mastoparan (VDWKKIGQHILSVL)
Polistes Mastoparan of Polistes jadwigae
Eumenitin (LNLKGIFKKVASLLT) (K+ > Cl- selectivity) (Arcisio-Miranda et al., 2008).
Eumenitin of Eumenes rubronotatus (P0C931)