Cell Penetration Properties of a Highly Efficient Mini  Maurocalcine Peptide

doi:10.3390/ph6030320

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Pharmaceuticals 2013, 6(3), 320-339; doi:10.3390/ph6030320

Article

Cell Penetration Properties of a Highly Efficient Mini Maurocalcine Peptide

Céline Tisseyre^1,2,3,†, Eloi Bahembera^1,2,3,†, Lucie Dardevet^1,2,3, Jean-Marc Sabatier⁴, Michel Ronjat^1,2,3 and Michel De Waard^1,2,4,5,*

¹ Unité Inserm U836, Grenoble Institute of Neuroscience, Université Joseph Fourier, La Tronche, Chemin Fortuné Ferrini, Bâtiment Edmond Safra, 38042 Grenoble Cedex 09, France ² Labex Ion Channel Science and Therapeutics, Nice, France ³ Université Joseph Fourier, Grenoble, France ⁴ Inserm U1097, Parc scientifique et technologique de Luminy, 163, avenue de Luminy, 13288 Marseille cedex 09, France ⁵ Smartox Biotechnology, Biopolis, 5 Avenue du Grand Sablon, 38700 La Tronche, France ^† These authors contributed equally to this work.

* Author to whom correspondence should be addressed.

Received: 23 February 2013; in revised form: 6 March 2013 / Accepted: 7 March 2013 / Published: 18 March 2013

(This article belongs to the Special Issue Cell-penetrating Peptides)

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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, MCa_UF1-9, 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 MCa_UF1-9 pH-sensitive. Greater cell penetration at acidic pH suggests that MCa_UF1-9 can be used to specifically target cancer cells in vivo where tumor masses grow in more acidic environments.

Keywords: maurocalcine; hadrucalcin; toxin; cell penetrating peptide; F98 cells; glioma; analogs

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MDPI and ACS Style

Tisseyre, C.; Bahembera, E.; Dardevet, L.; Sabatier, J.-M.; Ronjat, M.; De Waard, M. Cell Penetration Properties of a Highly Efficient Mini Maurocalcine Peptide. Pharmaceuticals 2013, 6, 320-339.

AMA Style

Tisseyre C, Bahembera E, Dardevet L, Sabatier J-M, Ronjat M, De Waard M. Cell Penetration Properties of a Highly Efficient Mini Maurocalcine Peptide. Pharmaceuticals. 2013; 6(3):320-339.

Chicago/Turabian Style

Tisseyre, Céline; Bahembera, Eloi; Dardevet, Lucie; Sabatier, Jean-Marc; Ronjat, Michel; De Waard, Michel. 2013. "Cell Penetration Properties of a Highly Efficient Mini Maurocalcine Peptide." Pharmaceuticals 6, no. 3: 320-339.

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