Venom Pathophysiology
The common European adder (Vipera berus berus) presents a critical biochemical challenge. Venom profiles are highly dynamic; substantial variations in proteomic composition occur not only across geographic ranges but also between melanistic (black) and normally coloured phenotypes and area where they live.
Hemostatic Disruption
Primary toxicity is driven by Phospholipase A2 (PLA2). Enzymes like Daboxin P homologs act as potent anticoagulants by binding to Factor X/Xa, disrupting the coagulation cascade. Simultaneously, svPLA2s induce intense local inflammation and nociception through mechanisms that are both catalytic-dependent and independent.
“Snake blood serum contains endogenous PLA2 inhibitors (PLIs), believed to protect against autointoxication. Alpha-type PLIs and acidic modulators like HPD-11 serve as the foundation for our synthetic neutralization strategies.”
Target Profile: P31854
Scientific Goal
Develop a chemically defined, non-immunogenic peptide framework to replace traditional polyclonal serotherapy.
Molecular Designer
Structure-based design for active site blockade.
Hydrophobic Core
Catalytic Warheads
Stabilisers
Sequence Analyzer Standby
Initialise peptide construction by selecting amino acids. A therapeutic sequence for the P31854 group IIA PLA2 requires hydrophobic anchors and a specific warhead residue.
Molecular Docking
The structural rationale for active-site inhibition.
Hydrophobic Anchor
Group IIA PLA2 enzymes feature a narrow hydrophobic channel. Synthetic inhibitors must contain a core of Leucine, Isoleucine, or Alanine to anchor within this cleft via van der Waals forces.
Catalytic Warhead
The warhead (e.g., Tyrosine or Arginine) replicates the interaction of the substrate. Tyr forms H-bonds with the His48/Asp49 catalytic dyad, effectively disabling the enzyme’s hydrolytic capacity.
Interfacial Binding Shield
Directly targets the active site channel to prevent the cleavage of the sn-2 fatty acyl bond in phospholipids.
Designed to be complementary to the interfacial binding surface (i-face), physically preventing the toxin from docking onto cell surfaces.
The RAPID System
A conceptual leap toward the Rapid on-site analyte-specific peptide intervention and diversion system for snakebite management.
Field Analysis
Diagnostic sensors identify specific toxin isoforms at the bite site to determine the required peptide profile.
Rapid Synthesis
Microwave-Assisted SPPS technology allows for automated production of personalised therapeutics on-demand.
Logistical Ease
Synthetic, chemically stable peptides eliminate the cold-chain logistical hurdles that hinder traditional antivenom distribution.
Global Health Equity
This framework shifts the paradigm from broad-spectrum biologicals to high-precision synthetic molecules, ensuring rapid emergency care across all geographic boundaries.