Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i>
<i>Hemiscorpius lepturus </i>scorpion stings do not induce considerable pain based on epidemiological surveys conducted in the southwest part of Iran. Accordingly, this study was aimed to identify the analgesic molecule in <i>H. lepturus</i> venom by analyzing a cDNA library...
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doaj-c82dd66128f848a3b1c550119c38b5cf2021-04-28T23:07:26ZengMDPI AGMolecules1420-30492021-04-01262580258010.3390/molecules26092580Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i>Sedigheh Bagheri-Ziari0Delavar Shahbazzadeh1Soroush Sardari2Jean-Marc Sabatier3Kamran Pooshang Bagheri4Venom and Biotherapeutics Molecules Laboratory, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 1316943551, IranVenom and Biotherapeutics Molecules Laboratory, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 1316943551, IranDrug Design and Bioinformatics Unit, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 1316943551, IranInstitute of NeuroPhysiopathology (INP), Faculté de Pharmacie, Université d’Aix-Marseille, UMR 7051, 27 Bd Jean Moulin, CEDEX 05, 13385 Marseille, FranceVenom and Biotherapeutics Molecules Laboratory, Medical Biotechnology Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran 1316943551, Iran<i>Hemiscorpius lepturus </i>scorpion stings do not induce considerable pain based on epidemiological surveys conducted in the southwest part of Iran. Accordingly, this study was aimed to identify the analgesic molecule in <i>H. lepturus</i> venom by analyzing a cDNA library of the scorpion venom gland looking for sequences having homology with known animal venom analgesic peptides. The analgesic molecule is a cysteine rich peptide of 55 amino acids. the synthetic peptide was deprotected and refolded. RP-HPLC, Ellman’s, and DLS assays confirmed the refolding accuracy. Circular dichroism (CD) showed helix and beta sheet contents. This peptide, called leptucin, demonstrated 95% analgesic activity at the dose of 0.48 mg/kg in hot plate assay. Leptucin at the doses of 0.32, 0.48, and 0.64 mg/kg showed 100% activity in thermal tail flick test. No hemolysis or cytotoxicity was observed at 8 and 16 µg. Histopathology evaluations indicated no hepatotoxicity, nephrotoxicity, and cardiotoxicity. We thus report that leptucin is the analgesic agent of <i>H. lepturus</i> venom. Regarding the high in vivo efficacy of leptucin and the fact it shows no observable toxicity, it could be suggested as a drug lead in a preclinical study of acute pain as well as the study of its mechanism of action.https://www.mdpi.com/1420-3049/26/9/2580leptucinanalgesic peptide<i>Hemiscorpius lepturus</i>scorpion |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sedigheh Bagheri-Ziari Delavar Shahbazzadeh Soroush Sardari Jean-Marc Sabatier Kamran Pooshang Bagheri |
spellingShingle |
Sedigheh Bagheri-Ziari Delavar Shahbazzadeh Soroush Sardari Jean-Marc Sabatier Kamran Pooshang Bagheri Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> Molecules leptucin analgesic peptide <i>Hemiscorpius lepturus</i> scorpion |
author_facet |
Sedigheh Bagheri-Ziari Delavar Shahbazzadeh Soroush Sardari Jean-Marc Sabatier Kamran Pooshang Bagheri |
author_sort |
Sedigheh Bagheri-Ziari |
title |
Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> |
title_short |
Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> |
title_full |
Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> |
title_fullStr |
Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> |
title_full_unstemmed |
Discovery of a New Analgesic Peptide, Leptucin, from the Iranian Scorpion, <i>Hemiscorpius lepturus</i> |
title_sort |
discovery of a new analgesic peptide, leptucin, from the iranian scorpion, <i>hemiscorpius lepturus</i> |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2021-04-01 |
description |
<i>Hemiscorpius lepturus </i>scorpion stings do not induce considerable pain based on epidemiological surveys conducted in the southwest part of Iran. Accordingly, this study was aimed to identify the analgesic molecule in <i>H. lepturus</i> venom by analyzing a cDNA library of the scorpion venom gland looking for sequences having homology with known animal venom analgesic peptides. The analgesic molecule is a cysteine rich peptide of 55 amino acids. the synthetic peptide was deprotected and refolded. RP-HPLC, Ellman’s, and DLS assays confirmed the refolding accuracy. Circular dichroism (CD) showed helix and beta sheet contents. This peptide, called leptucin, demonstrated 95% analgesic activity at the dose of 0.48 mg/kg in hot plate assay. Leptucin at the doses of 0.32, 0.48, and 0.64 mg/kg showed 100% activity in thermal tail flick test. No hemolysis or cytotoxicity was observed at 8 and 16 µg. Histopathology evaluations indicated no hepatotoxicity, nephrotoxicity, and cardiotoxicity. We thus report that leptucin is the analgesic agent of <i>H. lepturus</i> venom. Regarding the high in vivo efficacy of leptucin and the fact it shows no observable toxicity, it could be suggested as a drug lead in a preclinical study of acute pain as well as the study of its mechanism of action. |
topic |
leptucin analgesic peptide <i>Hemiscorpius lepturus</i> scorpion |
url |
https://www.mdpi.com/1420-3049/26/9/2580 |
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