The crystal and molecular structure of a toxin from the scorpion Centruroides sculpturatus has been solved by standard x-ray crystallographic methods at 3 A resolution. Subsequently the 3 A model has been refined and the resolution has been extended to 1.8 A using the gradient-curvature method. The final reliability index of 0.17 The structure has two and a half turns of alpha-helix, a three-strand stretch of antiparallel beta-sheet and several beta-turns. Three of the four disulfide bridges are found in close interaction with the alpha-helix and beta-sheet structures in what constitutes a very rigid part of the molecule. Examination of available scorpion toxin sequences reveals several sections containing invariant and/or semiinvariant amino acids. Many of these residues are found clustered on a rather large flat surface which is also clearly more hydrophobic than other areas on the molecule. These observations suggest that this surface may play a role in the biological action of scorpion toxins. Secondary structure predictions calculated using the method of Dufton and Hider agree well with the x-ray structure. This is also true for other scorpion toxins and reinforces the idea that scorpion toxins are a family of structurally related proteins.
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http://dx.doi.org/10.1016/0041-0101(82)90137-4 | DOI Listing |
Toxicon
January 2025
Laboratory of Experimental Pathophysiology, Universidade Do Extremo Sul Catarinense. Universitário, 88806-000. Criciúma. Santa Catarina, Brazil. Electronic address:
Tityus serrulatus accident promote vast symptomatology related to toxins of the venom, which leads to a massive release of neurotransmitters, notably dopamine, affecting behavior and neurochemistry. The recommended treatment for envenomation is the antiscorpionic serum (SAEsc) administration. Related to this complexity of the Tityus serrulatus envenomation, this study aimed to assess organism responses to the venom, its impact on behavior, oxidative stress, neurochemistry, and genetic impacts, as well as the efficacy of SAEsc, especially concerning dopamine levels and genetic interactions.
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January 2025
Laboratory of Venoms and Toxins, Pasteur Institute of Morocco. Electronic address:
Scorpion fauna is abundant in regions with arid and semi-arid climates, exposing these areas to a risk of envenomation, especially for children. Scorpion envenomations cause thousands of deaths each year, with notable incidences in the MENA region, South America, Latin and Central America, and India. Morocco is one of the countries most affected by this phenomenon; according to statistics from the Moroccan Poison Control and Pharmacovigilance Center (CAPM), approximately 8,565 scorpion stings and envenomations were recorded annually between 2016 and 2022, mainly among children.
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January 2025
Venom and Biotherapeutics Molecules Lab., Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. Electronic address:
Scorpion envenomation, especially from Hemiscorpius lepturus, poses a significant health risk, leading to considerable morbidity and mortality. The venom's major toxin, which includes phospholipase D (PLD), is responsible for various systemic complications. In prior studies, we identified a native phospholipase D (PLD) toxin as a key lethal factor in the venom of H.
View Article and Find Full Text PDFZhongguo Xue Xi Chong Bing Fang Zhi Za Zhi
December 2024
Mongolian Medical College, Inner Mongolia Minzu University; National Medical Products Administration Key Laboratory of Quality Control of Traditional Chinese Medicine (Mongolian Medicine), Tongliao, Inner Mongolia 028043, China.
Scorpion venom is a highly complicated cocktail of bioactive components including mucoproteins, enzymes, lipids, bioactive peptides, and other organic or inorganic molecules. Scorpion venom antimicrobial peptides are a class of small-molecule bioactive peptides extracted from scorpion venoms, which have shown a variety of biological activities, including antiviral, antibacterial, antifungal and antitumor actions. This review describes the progress of researches on the antiparasitic activities of scorpion venoms and their antimicrobial peptides, so as to provide insights into the research and development of novel antiparasitic agents.
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December 2024
Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Scorpion venom contains various bioactive peptides, many of which exhibit insecticidal activity. The majority of these peptides have a cystine-stabilized α-helix/β-sheet (CSαβ) motif. In addition to these peptides, scorpion venom also contains those with a cystine-stabilized α-helix/α-helix (CSαα) motif, which are known as κ-KTx peptides.
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