Bioassay of derived components from venom of Iranian medically important scorpions to identify the bradykinin potentiating factors

Abstract

Abstract:The venom of animals, including snakes, scorpions and spiders is a complex combination of proteins, peptides, and other biomolecules as well as some minerals. Among the biomolecules, some peptides prevent converting of angiotensin 1 to angiotensin 2 by inhibiting of the Angiotensin Converting Enzyme (ACE) and finally reducing the blood pressure in the victims. The aim of the present study was to isolate venom components of the three species of Iranian medically important scorpions and to study the bradykinin potentiating effect of them. Separation of the venom components for each scorpion was carried out using high performance liquid chromatography (HPLC). The range of fractions (zones) obtained in several replicates on Guinea pig ileum and rat uterus tissues were performed using organ bath instrument. The bioassays were resulted in the peptides including Z 1 and Z 2 regions of venom chromatogram of the Hottentotta sulcyi, Z 2 for Odontobutus doriea and Z 2 and Z 3 in Mesobutus eupeus venom demonstrated bradykinin potentiating effect.

Scorpion Venom as a Source of Antimicrobial Peptides: Overview of Biomolecule Separation, Analysis and Characterization Methods

“…The collected fractions were evaluated for their smooth muscle contracting ability on the guinea pig ileum and rat uterus. Thus, results confirmed the presence of bradykinin potentiating peptides in the venom of the three scorpions, illustrating the use of the above-mentioned fractionation scheme for making such peptides available in the quantities needed for further molecular and structural studies [87]. Interestingly, the implementation of bioassay-guided fractionation has underscored its effectiveness in isolating and characterizing biologically significant compounds present in scorpion venom.…”

Scorpion Venom–Toxins that Aid in Drug Development: A Review

“…Bradykinin potentiating scorpion venom peptides are devoid of disulphide bridges and enriched with proline residues at the C-terminus (Goudarzi et al 2017). Studies report that proline enrichment at the C-terminal end contributes in its increased bradykinin potentiating activity (Goudarzi et al 2017).…”

“…Bradykinin potentiating scorpion venom peptides are devoid of disulphide bridges and enriched with proline residues at the C-terminus (Goudarzi et al 2017). Studies report that proline enrichment at the C-terminal end contributes in its increased bradykinin potentiating activity (Goudarzi et al 2017). A unique characteristic of these peptides is that their functioning involves a synergistic action or bradykinin proteolysis prevention (Rioli et al 2008).…”

“…These peptides are notable for being strong hypotensive agents (Petricevich et al 2013). Further studies on T. serrulatus reveal that its bradykinin potentiating activity regulates blood pressure as bradykinin receptor synthesis and ACE activity is averted (Goudarzi et al 2017…”

Mass-Spectrometry-Based Lipidome and Proteome Profiling of Hottentotta saulcyi (Scorpiones: Buthidae) Venom

“…In this study, we employed liquid chromatography tandem mass spectrometry (LC-MS/MS)-based proteomic and lipidomic approaches to explore the molecular diversity of the yet unstudied venom of H. saulcyi. With a median lethal dose (LD50) value (intravenous administration) of 0.73 mg/kg (Turkey) [24], 1.07 mg/kg (Iraq) [25], and 1.01 mg/kg (Iran) [26] in the laboratory mice (20 ± 2 g), the H. saulcyi venom seems to be one of the family's most toxic species, and accidents with the species can be dangerous to humans in the distributed area including Iran, Iraq, Syria, Turkey and Afghanistan. Despite the close similarities in LD50 value, intraspecies venom variation has been reported in scorpion specimens [27][28][29], which can result from, e.g., evolutionary history, climatic factors, ontogeny, or adaptation toward different prey.…”