J. Muller, L. Y. Chan, M. C. Toffoli-Kadri, M. Mortari, D. Craik, J. Koehbach
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Abstract 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 α-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.
期刊介绍:
Toxin Reviews provides an international forum for publishing state-of-the-art reviews and guest-edited single topic special issues covering the multidisciplinary research in the area of toxins derived from animals, plants and microorganisms. Our aim is to publish reviews that are of broad interest and importance to the toxinology as well as other life science communities. Toxin Reviews aims to encourage scientists to highlight the contribution of toxins as research tools in deciphering molecular and cellular mechanisms, and as prototypes of therapeutic agents. Reviews should emphasize the role of toxins in enhancing our fundamental understanding of life sciences, protein chemistry, structural biology, pharmacology, clinical toxinology and evolution. Prominence will be given to reviews that propose new ideas or approaches and further the knowledge of toxinology.