Journal
TOXIN REVIEWS
Volume 42, Issue 1, Pages 362-381Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15569543.2022.2065510
Keywords
Pain; antinociceptive; peptide; venom
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This review highlights the structural diversity of antinociceptive arthropod peptides and emphasizes their vast potential for the discovery of novel analgesic lead molecules.
Many analgesic peptides have been isolated from arthropod species such as spiders and scorpions and their three-dimensional structures, which are typically stabilized by several disulfide-bonds, correlate with their activity and molecular targets. In contrast, only individual species of Chilopoda (centipedes) and Insecta (Hymenoptera) have been described to contain antinociceptive peptides and those display only alpha-helical structures, with the latter also lacking disulfide bonds. Here we review the structural diversity of antinociceptive arthropod peptides and highlight their largely untapped potential for the discovery of novel analgesic lead molecules.
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