Recombinant Vipera aspis aspis Snake venom vascular endothelial growth factor toxin
Description
Definition and Classification
Recombinant Vipera aspis aspis snake venom vascular endothelial growth factor toxin refers to a laboratory-produced version of the VEGF-F protein derived from the venom of the asp viper (Vipera aspis aspis). VEGF-Fs are exogenous members of the VEGF family, distinct from endogenous VEGF-A in vertebrates, and are characterized by their ability to bind vascular endothelial growth factor receptors (VEGFRs) with high affinity . These toxins are implicated in enhancing vascular permeability, inducing hypotension, and modulating angiogenesis .
Functional Properties
Recombinant VEGF-Fs demonstrate multifaceted bioactivities:
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Vascular Permeability: VEGF-Fs induce rapid vascular leakage, exceeding the potency of human VEGF-A .
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Receptor Activation: Bind selectively to VEGFR2 (KDR) or VEGFR1 (Flt-1), depending on species-specific structural variations .
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Immune Modulation: Recruitment of neutrophils and lymphocytes, as observed in Crotalus durissus terrificus VEGF (CdtVEGF) .
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Angiogenesis: Promote endothelial cell proliferation and migration in vitro .
PEGylation of recombinant CdtVEGF reduced inflammatory activity while retaining angiogenic potential, suggesting therapeutic utility .
4.2. Therapeutic Applications
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Cancer Therapy: VEGF-Fs’ angiogenic properties could be harnessed for tumor vascularization studies .
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Ischemic Diseases: Potential use in promoting collateral vessel formation in ischemic heart disease .
Research Gaps and Challenges
Comparative Analysis with Other Viper Venoms
| Species | VEGF-F Abundance | Key Functional Traits | Clinical Impact |
|---|---|---|---|
| Vipera aspis aspis | ~4–8% of venom | Hypotensive, pro-inflammatory | Local edema, systemic shock |
| Daboia russelii | 5–10% of venom | KDR-specific, strong vascular leakage | Coagulopathy |
| Montivipera xanthina | 3–5% of venom | Flt-1 preference, weak heparin binding | Tissue necrosis |
Product Specs
Target Background
Q&A
Experimental Design for Studying Recombinant Vipera aspis aspis Snake Venom VEGF Toxin
Q: How should one design an experiment to study the effects of recombinant Vipera aspis aspis snake venom vascular endothelial growth factor toxin on vascular permeability? A:
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Objective: Investigate the toxin's ability to increase vascular permeability.
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Methodology:
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Cell Culture: Use endothelial cells (e.g., HUVECs) in a controlled environment.
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Toxin Administration: Apply varying concentrations of the recombinant toxin to the cells.
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Permeability Assay: Utilize a permeability assay (e.g., FITC-dextran) to measure changes in vascular permeability.
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Data Analysis: Compare results across different toxin concentrations to assess dose-response effects.
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Data Contradiction Analysis in VEGF Toxin Studies
Q: How can researchers address contradictions in data regarding the effects of Vipera aspis aspis snake venom VEGF toxin on vascular endothelial cells? A:
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Approach:
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Literature Review: Conduct a thorough review of existing studies to identify potential sources of variability (e.g., toxin concentration, cell type).
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Experimental Replication: Replicate studies with standardized conditions to verify findings.
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Statistical Analysis: Use meta-analysis or statistical modeling to reconcile disparate results.
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Advanced Research Questions: Mechanisms of Action
Q: What are the key mechanisms by which recombinant Vipera aspis aspis snake venom VEGF toxin exerts its effects on vascular endothelial cells? A:
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Mechanisms:
Comparative Analysis of Venom-Type VEGFs
Q: How do venom-type VEGFs from different snake species (e.g., Vipera aspis, Bothrops insularis) compare in terms of structure and function? A:
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Comparison:
Genomic Evolution of Venom-Type VEGFs
Q: What insights do genomic analyses provide into the evolution of venom-type VEGF genes in snakes? A:
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Evolutionary Insights:
Methodological Considerations for Recombinant Protein Production
Q: What are the key methodological considerations for producing recombinant Vipera aspis aspis snake venom VEGF toxin in Escherichia coli? A:
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Production Methodology:
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Cloning: Clone the VEGF toxin gene into an appropriate plasmid.
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Expression: Express the protein in E. coli, potentially using a His-tag for purification.
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Purification: Use Ni(2+)-affinity chromatography for purification.
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Refolding: Refold the protein to achieve its active form, as it may be produced as an insoluble monomer .
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Applications in Cancer Research
Q: How can recombinant Vipera aspis aspis snake venom VEGF toxin be utilized in cancer research, particularly for targeting tumor endothelium? A:
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Application:
Safety and Handling Precautions
Q: What safety and handling precautions should researchers take when working with recombinant Vipera aspis aspis snake venom VEGF toxin? A:
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Precautions:
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Personal Protective Equipment (PPE): Wear appropriate PPE, including gloves and lab coats.
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Biosafety Level: Ensure work is conducted at an appropriate biosafety level.
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Waste Disposal: Follow proper protocols for disposing of biological waste.
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Material Safety Data Sheets (MSDS): Consult MSDS for specific handling instructions .
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Northern Blot Analysis for Venom-Type VEGFs
Q: How can Northern blot analysis be used to study the distribution of venom-type VEGFs in snake species? A:
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Methodology:
Future Research Directions
Q: What are potential future research directions for studying recombinant Vipera aspis aspis snake venom VEGF toxin? A:
