ArticleProceedings of the National Academy of Sciences of the United States of America1995
Scorpion toxins as natural scaffolds for protein engineering.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 153 citations in OpenAlex.
- Oleocanthal as a Multifunctional Anti-Cancer Agent: Mechanistic Insights, Advanced Delivery Strategies, and Synergies for Precision Oncology.International journal of molecular sciences · 2025Review
- An Engineered β-Hairpin Peptide Forming Thermostable Complexes with ZnChembiochem : a European journal of chemical biology · 2023Article
- Opening the HIV envelope: potential of CD4 mimics as multifunctional HIV entry inhibitors.Current opinion in HIV and AIDS · 2020Review
- An efficient, step-economical strategy for the design of functional metalloproteins.Nature chemistry · 2019Article
- Molecular Dynamics Simulation Reveals Specific Interaction Sites between Scorpion Toxins and KToxins · 2017Article
- Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold.Scientific reports · 2017Article
- PredSTP: a highly accurate SVM based model to predict sequential cystine stabilized peptides.BMC bioinformatics · 2015Article
- Structure and function of μ-conotoxins, peptide-based sodium channel blockers with analgesic activity.Future medicinal chemistry · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
- Designing hydrolytic zinc metalloenzymes.Biochemistry · 2014Review
- Article
- Animal toxins influence voltage-gated sodium channel function.Handbook of experimental pharmacology · 2014Review
- Influence of active site location on catalytic activity in de novo-designed zinc metalloenzymes.Journal of the American Chemical Society · 2013Article
- Scorpion toxins specific for potassium (K+) channels: a historical overview of peptide bioengineering.Toxins · 2012Review
- Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope.Journal of molecular biology · 2012Article
- Article
- Computational approaches for rational design of proteins with novel functionalities.Computational and structural biotechnology journal · 2012Review
- Hydrolytic catalysis and structural stabilization in a designed metalloprotein.Nature chemistry · 2011Article
- Miniproteins as phage display-scaffolds for clinical applications.Molecules (Basel, Switzerland) · 2011Review
- Elicitation of structure-specific antibodies by epitope scaffolds.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A compact, well-organized, and natural motif, stabilized by three disulfide bonds, is proposed as a basic scaffold for protein engineering. This motif contains 37 amino acids only and is formed by a short helix on one face and an antiparallel triple-stranded beta-sheet on the opposite face. It has been adopted by scorpions as a unique scaffold to express a wide variety of powerful toxic ligands with tuned specificity for different ion channels. We further tested the potential of this fold by engineering a metal binding site on it, taking the carbonic anhydrase site as a model. By chemical synthesis we introduced nine residues, including three histidines, as compared to the original amino acid sequence of the natural charybdotoxin and found that the new protein maintains the original fold, as revealed by CD and 1H NMR analysis. Cu2+ ions are bound with Kd = 4.2 x 10(-8) M and other metals are bound with affinities in an order mirroring that observed in carbonic anhydrase. The alpha/beta scorpion motif, small in size, easily amenable to chemical synthesis, highly stable, and tolerant for sequence mutations represents, therefore, an appropriate scaffold onto which polypeptide sequences may be introduced in a predetermined conformation, providing an additional means for design and engineering of small proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.