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2000
Volume 2, Issue 1
  • ISSN: 2666-1217
  • E-ISSN: 2666-1225

Abstract

( ) is one of the most hazardous scorpions in Morocco and has a highly toxic venom responsible for severe cases of envenomation. However, few studies have focused on deciphering its proteic composition.

Herein, we aim to map out the complete proteome of the venom filtrate to highlight its complexity and the polymorphism of its toxic content. This, in turn, will lead to a deeper understanding of the toxins’ mechanism of action and will help uncover those with therapeutic potential.

Top-down and bottom-up proteomic approaches were used complementarily to decipher the proteome of the venom. These approaches were carried out on nano-high liquid chromatography coupled to nano-electrospray tandem mass spectrometry (Nano-LC-ESI-MS/MS).

venom encloses a complex mixture of 269 different compounds with molecular weights ranging from 1618.74 to 14 214.84 Da. The most abundant ones showed masses from 6185.92 to 7899.53 Da (53.89%) followed by those ranging from 2079.25 to 5969.63 Da (37.81%). Interestingly, the combination of the results of both approaches allowed the screening of a total of 112 peptides. The highest percentage was represented by neuropeptides (87%), including NaTxs, KTxs, ClTxs, venom proteins, venom neuropeptides, and myotropic neuropeptides. Moreover, other peptides were identified, such as antimicrobial peptides, amphipathic peptides, cysteine-rich venom peptides, enzymes, kunitz-type inhibitors and orphan peptides.

The venom appears to contain a great number of diverse peptides, some of which could prospectively be exploited for their pharmaceutical potential.

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Keyword(s): Androctonus mauretanicus scorpion; bottom-up; Scorpion venom; top-down; toxins; venomic
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