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2000
Volume 21, Issue 6
  • ISSN: 1570-1646
  • E-ISSN: 1875-6247

Abstract

Background and Objectives

Venomous scorpions play a crucial role in medicine and public health. scorpion is known as one of the most populous species in East Asia and Iran, while its venom proteome has still not been fully determined.

Aims

In the current research, the proteomic profile of scorpion venom to determine the structural and functional characteristics of its compounds used for treatment will be examined for the first time.

Methods

2D-PAGE, HPLC, SDS-PAGE, sequencing, and MALDI-TOF MS techniques were used to investigate the properties of these peptides.

Results

The 2D-PAGE analysis of crude toxin from revealed a minimum of 96 protein spots, with isoelectric points ranging from 4 to 9 and molecular weights spanning from 3.6 to 205 kDa. Following this, HPLC was used to isolate 14 fractions of crude toxins, and the protein content of these fractions was measured. SDS-PAGE analysis identified 7 protein bands within the crude toxin fractions, with molecular weights ranging from 13 to 217 kDa. Further examination of fraction 7 through amino acid sequencing resulted in the identification of two protein bands labeled peptide 3 and peptide 4. Ultimately, these protein bands were extracted, and their molecular mass and amino acid sequences were analyzed using MALDI-TOF MS.

Conclusion

According to our results, the alignment of P3 and P4 protein sequences revealed the highest similarity to chrysophsin 2 and pheromone-bound protein 2, respectively.

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Two Novel Peptides from Buthotus saulcyi Scorpion Venom: Proteomic Analysis and Approaches
Curr. Proteomics 21, 843 (2024); https://doi.org/10.2174/0115701646354270250114111820
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  • Article Type:     Research Article
Keyword(s): Buthotus saulcyi; MALDI-TOF/MS; peptide; proteomic; scorpion; venom

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