Academic Journals Database
Disseminating quality controlled scientific knowledge

Cell Penetration Properties of a Highly Efficient Mini Maurocalcine Peptide

ADD TO MY LIST
 
Author(s): Céline Tisseyre | Eloi Bahembera | Lucie Dardevet | Jean-Marc Sabatier | Michel Ronjat | Michel De Waard

Journal: Pharmaceuticals
ISSN 1424-8247

Volume: 6;
Issue: 3;
Start page: 320;
Date: 2013;
Original page

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

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.
Why do you need a reservation system?      Affiliate Program