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Cell Penetrating Peptides

Recent research from the groups of Professors Mark Distefano and George Barany done in collaboration with Professor Elizabeth Wattenberg.

Prenylation is a common post-translational protein modification in eukaryotic cells. When prenylation occurs an enzyme adds a 15 or 20 carbon chain near the C-terminus of a protein. The modification controls the protein’s localization inside of the cell and is involved in directing other cellular events including some that are involved in the regulation of cancer proliferation.

Currently researchers in the Distefano lab have discovered other interesting properties of prenylated molecules. Their research has uncovered a series of prenylated peptides that have cell penetrating properties. These peptides could open the door for further study on the properties of larger prenylated proteins in cells, including these proteins’ participation in cellular signaling pathways involved in cancer proliferation. This information could lead to new cancer therapies and strategies for cancer prevention.

Cell penetrating peptides were prepared by Dan Mullen of Professor Barany’s group and James Wollack of the Distefano group. The cell penetrating properties of these peptides were investigated in Professor Wattenberg’s group by her student Nicholette Zeliadt in collaboration with James Wollack.

Right: HeLa cells treated with the pictured peptide. Green areas are the peptide localized between the nucleus and the plasma membrane. The plasma membrane is stained red and the nucleus is stained blue.

Left:A fluorescently labeled cell penetrating prenylated peptide


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