Scorpion venom peptides without disulfide bridges.
Several hundred disulfide-bridged neurotoxic peptides have been characterized from scorpion venom; however, only few scorpion venom peptides without disulfide bridges have been identified and characterized. These non-disulfide-bridged peptides (NDBPs) are a novel class of molecules because of their unique antimicrobial, immunological or cellular signaling activities. This review provides an overview of their structural simplicity, precursor processing, biological activities and evolution, and sheds insight into their potential clinical and agricultural applications. Based on their pharmacological activities and peptide size similarity, we have classified these peptides into six subfamilies.
Zeng
Xian-Chun
XC
Department of Biotechnology, Key Laboratory of MOE for Virology, Institute of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, P. R. China. zengx@mail.nih.gov
Corzo
Gerardo
G
Hahin
Richard
R
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism; D001920:Bradykinin / Q000378:metabolism; D040461:Gene Components; D006461:Hemolysis / Q000502:physiology; D007155:Immunologic Factors / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D010802:Phylogeny; D017433:Protein Structure, Secondary; D012604:Scorpion Venoms / Q000737:chemistry* / Q000235:genetics; D012605:Scorpions / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D007155:Immunologic Factors; D010455:Peptides; D012604:Scorpion Venoms; D001920:Bradykinin