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Function and Solution Structure of Huwentoxin-IV, a Potent Neuronal Tetrodotoxin (TTX)-sensitive Sodium Channel Antagonist from Chinese Bird Spider Selenocosmia huwena *
After comparison with other toxins purified from the same species, it is convinced that the positively charged residues of loop IV (residues 25–29), especially residue Arg-26, must be crucial to its binding to the neuronal tetrodotoxin-sensitive voltage-gated sodium channel.
Structure-Activity Relationships of Hainantoxin-IV and Structure Determination of Active and Inactive Sodium Channel Blockers*
It is hypothesized that residues Lys27, Arg29, His28, Lys32, Phe5, and Trp30 clustered on one face of HNTX-IV were responsible for ligand binding, and suggested that Lys27 and Arg29 were critical for the bioactivities.
Chemical Punch Packed in Venoms Makes Centipedes Excellent Predators*
The high level of biochemical diversity revealed in this study suggests that centipede venoms might be attractive subjects for prospecting and screening for peptide candidates with potential pharmaceutical or agrochemical applications.
The Venom Gland Transcriptome of Latrodectus tredecimguttatus Revealed by Deep Sequencing and cDNA Library Analysis
A gland transcriptome profile is provided and the understanding of the toxinome of spiders and coordination mechanism for toxin production in protein expression quantity is extended.
Synthesis and Analgesic Effects of μ-TRTX-Hhn1b on Models of Inflammatory and Neuropathic Pain
It is demonstrated that μ-TRTX-Hhn1b efficiently alleviated acute inflammatory pain and chronic neuropathic pain in animals and provided an attractive template for further clinical analgesic drug design.
Structure and Function of Hainantoxin-III, a Selective Antagonist of Neuronal Tetrodotoxin-sensitive Voltage-gated Sodium Channels Isolated from the Chinese Bird Spider Ornithoctonus hainana*
The results show that HNTX-III is distinct from β-scorpion toxins and other β-spider toxins in its mechanism of action and binding specificity and affinity, and contributes to the understanding of the mechanism of toxin-sodium channel interaction.
Shellfish Toxins Targeting Voltage-Gated Sodium Channels
An overview of the structure, bioactivity, and pharmacology of shellfish toxins that act on VGSCs are provided, along with a brief discussion on their pharmaceutical potential for pain management.