ArticlePharmaceuticals (Basel, Switzerland)2013
Cell penetration properties of a highly efficient mini maurocalcine Peptide.
Article in Pharmaceuticals (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Old dog, new trick: Charybdotoxin as a novel ryanodine receptor blocker.The Journal of physiology · 2026Article
- Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential.International journal of molecular sciences · 2025Review
- Exploring the Chemical Features and Biomedical Relevance of Cell-Penetrating Peptides.International journal of molecular sciences · 2024Review
- Review
- Research Progress Evaluating the Function and Mechanism of Anti-Tumor Peptides.Cancer management and research · 2020Review
- CPP-Ts: a new intracellular calcium channel modulator and a promising tool for drug delivery in cancer cells.Scientific reports · 2018Article
- Toxin bioportides: exploring toxin biological activity and multifunctionality.Cellular and molecular life sciences : CMLS · 2017Review
- 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
- FRET-Based Nanobiosensors for Imaging Intracellular Ca²⁺ and H⁺ Microdomains.Sensors (Basel, Switzerland) · 2015Article
- Scorpion venom components as potential candidates for drug development.Toxicon : official journal of the International Society on Toxinology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maurocalcine is a highly potent cell-penetrating peptide isolated from the Tunisian scorpion Maurus palmatus. Many cell-penetrating peptide analogues have been derived from the full-length maurocalcine by internal cysteine substitutions and sequence truncation. Herein we have further characterized the cell-penetrating properties of one such peptide, MCaUF1-9, whose sequence matches that of the hydrophobic face of maurocalcine. This peptide shows very favorable cell-penetration efficacy compared to Tat, penetratin or polyarginine. The peptide appears so specialized in cell penetration that it seems hard to improve by site directed mutagenesis. A comparative analysis of the efficacies of similar peptides isolated from other toxin members of the same family leads to the identification of hadrucalcin's hydrophobic face as an even better CPP. Protonation of the histidine residue at position 6 renders the cell penetration of MCaUF1-9 pH-sensitive. Greater cell penetration at acidic pH suggests that MCaUF1-9 can be used to specifically target cancer cells in vivo where tumor masses grow in more acidic environments.
Identifiers
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Registered trials
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.