1.C.124. The Antimicrobial Pore-forming Pandinin (Pin) Family
Pandinin 2 (Pin2) is a pore-forming α-helical polycationic peptide from the venom of the African scorpion, Pandinus imperator, with high antimicrobial activity against Gram-positive bacteria but less active against Gram-negative bacteria (Nomura et al. 2004, Belokoneva et al. 2004). However it has strong hemolytic activity against sheep red blood cells. In the chemically synthesized Pin2GVG analog, the GVG motif minimizes its hemolytic activity while maintaining its antimicrobial activity (Velasco-Bolom et al. 2017).
The membrane disruption mechanism of the antimicrobial peptide from the venom of the African scorpion, pandinin 1 (pin1) has been studied, showing that the two α-helical regions move around the central hinge region, which contains Pro19. 31P NMR spectra of lipid membranes in the presence of pin1, at various temperatures, showed that pin1 induces various lipid phase behaviors depending on the acyl chain length and charge of phospholipids. pin1 is located at the membrane-water interface approximately parallel to the bilayer surface. Solid-state NMR results correlated well with the observed biological activity of pin1 in red blood cells and bacteria (Nomura et al. 2005).