ArticleThe Journal of biological chemistry2010
D-Maurocalcine, a pharmacologically inert efficient cell-penetrating peptide analogue.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential.International journal of molecular sciences · 2025Review
- Review
- Diagnostic and Therapeutic Value of Aptamers in Envenomation Cases.International journal of molecular sciences · 2020Review
- Cell-penetrating peptides derived fromThe Journal of biological chemistry · 2018Article
- Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands.The Journal of general physiology · 2016Article
- In cellulo phosphorylation induces pharmacological reprogramming of maurocalcin, a cell-penetrating venom peptide.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Biodistribution, Stability, and Blood Distribution of the Cell Penetrating Peptide Maurocalcine in Mice.International journal of molecular sciences · 2015Article
- Cell penetration properties of a highly efficient mini maurocalcine Peptide.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Small efficient cell-penetrating peptides derived from scorpion toxin maurocalcine.The Journal of biological chemistry · 2012Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maurocalcine has been the first demonstrated animal toxin acting as a cell-penetrating peptide. Although it possesses competitive advantages, its use as a cell-penetrating peptide (CPP) requires that analogues be developed that lack its characteristic pharmacological activity on ryanodine-sensitive calcium channels without affecting its cell-penetrating and vector efficiencies. Here, we present the synthesis, three-dimensional (1)H NMR structure, and activity of D-maurocalcine. We demonstrate that it possesses all of the desired features for an excellent CPP: preserved structure, lack of pharmacological action, conserved vector properties, and absence of cell toxicity. This is the first report of a folded/oxidized animal toxin in its D-diastereomer conformation for use as a CPP. The protease resistance of this new peptide analogue, combined with its efficient cell penetration at concentrations devoid of cell toxicity, suggests that D-maurocalcine should be an excellent vector for in vivo applications.
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