Snake- and spider-venom-derived toxins as lead compounds for drug development

Keyphrases

• Drug Development 100%
• Snake Venom 100%
• Spider Venom 100%
• Peptide Toxin 66%
• Pharmacodynamic Interactions 33%
• Cell Membrane 33%
• Gene Duplication 33%
• Biocompatibility 33%
• Protein Channel 33%
• Immunogenic 33%
• Protease 33%
• Molecular Targets 33%
• Nervous System 33%
• Chemical Structure 33%
• Peptide Sequencing 33%
• Venom 33%
• Therapeutic Importance 33%
• Peptide Scaffold 33%
• Process Optimization 33%
• Biodegradability 33%
• Disulfide Bridge 33%
• Defense Mechanisms 33%
• Pharmacological Tools 33%
• Physiological Systems 33%
• Pharmacokinetic Properties 33%
• Therapeutic Effect 33%
• Protein Receptor 33%
• Membrane Ion Channels 33%
• Protein Toxin 33%
• Clinical Development 33%
• Snake Toxin 33%
• Ionic Channels 33%
• Coagulation Cascade 33%
• Scaffold Structure 33%
• Highly Tunable 33%
• Pharmaceutical Properties 33%
• Toxic Peptides 33%
• Venom Toxins 33%
• Venom Peptides 33%
• New Molecular Entity 33%

Pharmacology, Toxicology and Pharmaceutical Science

• Drug Development 100%
• Snake Venom 100%
• Lead Compound 100%
• Spider Toxin 100%
• Ion Channel 66%
• Prey 66%
• Pharmacodynamics 33%
• Receptor 33%
• Biocompatibility 33%
• Molecular Target 33%
• Disulfide 33%
• Therapeutic Effect 33%
• Protein Toxins 33%
• Receptor Protein 33%
• Pharmacokinetics 33%
• Diseases 33%

Biochemistry, Genetics and Molecular Biology

• Spider Toxin 100%
• Drug Development 100%
• Prey 66%
• Ion Channel 66%
• Cell Membrane 33%
• Gene Duplication 33%
• Peptide Sequence 33%
• Process Optimization 33%
• Disulfide 33%
• Pharmacodynamics 33%
• Chemical Structure 33%
• Protease 33%
• Pharmacokinetic Properties 33%
• Biodegradability 33%