Investigation of the sequence and length dependence for cell-penetrating prenylated peptides

James W. Wollack, Nicholette A. Zeliadt, Joshua D. Ochocki, Daniel G. Mullen, George Barany, Elizabeth V. Wattenberg, Mark D. Distefano

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

Cell penetrating peptides are useful delivery tools for introducing molecules of interest into cells. A new class of cell penetrating molecules has been recently reported-cell penetrating, prenylated peptides. In this study a series of such peptides was synthesized to examine the relationship between peptide sequence and level of peptide internalization and to probe their mechanism of internalization. This study revealed that prenylated peptides internalize via a non-endocytotic pathway regardless of sequence. Sequence length and identity was found to play a role in peptide uptake but prenylated sequences as short as two amino acids were found to exhibit significant cell penetrating properties.

Original languageEnglish (US)
Pages (from-to)161-163
Number of pages3
JournalBioorganic and Medicinal Chemistry Letters
Volume20
Issue number1
DOIs
StatePublished - Jan 1 2010

Keywords

  • Cell-penetrating peptide
  • Geranylgeranyl
  • Lipid modification
  • Posttranslational modification
  • Prenylataion
  • Prenylated peptide

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