Charybdotoxin Scaffold Introduction

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As a pioneer of charybdotoxin discovery, <strong>Creative Biolabs</strong> is pleased to offer our most extensive experience and the best services for boosting our clients’ research and project. </p> <p> Charybdotoxin (CTX) is a kind of neurotoxin isolated from the venom of the Israeli scorpion <em>Leiurus quinquestriatus hebraeus </em>(Deathstalker). It is a 37 amino acid (4 kDa) motif with the molecular formula C176H277N57O55S7. Functionally, charybdotoxin can block the calcium-activated potassium channels, which causes hyperexcitability of the nervous system. In addition, the structure analysis of charybdotoxin indicated an antiparallel triple-stranded β-sheet on one face, a short α-helix on the opposite face and three disulfide bonds in the interior core to form a conformationally stabilized structure. Besides that, it is a perfect example of cysteine-stabilized α-helical (CSH) and β-sheet (CSB) motifs, thus it is also termed as “cysteine-stabilized ab motif”. </p> <p> Charybdotoxin represents a source of small and stable scaffold which can bind to the biological targets with high affinity and specificity. According to the well-defined structure and function, charybdotoxin is able to be used as a natural scaffold for protein engineering. For instance, β-turn loop randomized charybdotoxin scaffold carried a CD4-like loop, which can serve as an underlying CD4 mimetic tool. The randomized charybdotoxin scaffold shown excellent affinity for HIV-1 gp120, which can lead to novel HIV-1 envelope binding activities and possibly HIV-1 antagonists by blocking the gp120-CD4 interaction (Li <em>et al.</em> 2001). With the modification of metal binding sites, charybdotoxin scaffold is also available to be induced the metal binding activity. </p> <p> As an improved phage display technology, Hi-Affi™ phage display platform has been used by <strong>Creative Biolabs</strong> for protein scaffold libraries construction. The technology is based on the expression of the recombinant peptide or protein as a fusion with a coated protein of bacteriophage then displaying on the phage surfaces to select specific binders. Combined with trimer codon technology and NNK method, our Hi-Affi™ phage display technology is more suitable for sorting and isolating the high affinity protein or peptide targets. It is available to expand the library affinity with 100% precise mutant and over 10<sup><span style="font-size:9px;">10</span></sup> diversity. </p> <p> <strong>Creative Biolabs</strong> is dedicated in the research of scaffold protein as well as scaffold library construction. Our most devoted scientists are confident in delivering libraries that meet all required specifications from customers. </p> <p class="ServiceShowPic"> <img src="static/img/scaffold-Charybdotoxin-Library-Construction.png" alt="Charybdotoxin Library Construction" /> <strong>Fig. 1</strong> Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. (<a href="http://www.rcsb.org/pdb/explore/explore.do?structureId=2CRD" target="_blank">PDB ID: 2CRD</a>) </p> <p class="Reference"> <strong>Reference</strong> </p> <ol class="ollist decimal Reference"> <li> Li, C.; <em>et al</em>. Phage randomization in a charybdotoxin scaffold leads to CD4‐mimetic recognition motifs that bind HIV‐1 envelope through non‐aromatic sequences. <em>The Journal of Peptide Research</em>. 2001, 57(6): 507-518. </li> </ol><br> <p class="pronote"><i class="fa fa-exclamation-triangle"></i>All listed services and products are For Research Use Only. 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Charybdotoxin Scaffold Introduction - Creative Biolabs