Solid-state NMR studies of antimicrobial peptides from arachnid venoms

Advances in peptide biochemistry and mass spectrometry as well as in peptide synthesis and NMR have permitted the isolation, identification and structure determination of numerous products from arachnid venoms, previously unexplored due to technical limitations. The chemical composition in arachnid venoms is diverse ranging from low molecular weight organic compounds such acylpolyamines to complex disulfide-rich peptides. A special group of spider and scorpion peptides are those amphipathic and positively charged structures with cytolytic properties. Their secondary structure is mostly alpha-helical, and they insert into the lipid cell membrane of eukaryotic or prokaryotic cells leading to the formation of pores and subsequently depolarizing the cell membrane of such cells. The mode of action and insertion of antimicrobial peptides from arachnid venoms represent an interesting source of natural molecules for clinical research. In this review, solid-state NMR studies to examine them will be described.