Efficient Delivery of Cyclic Peptides into Mammalian Cells with Short Sequence Motifs

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Author list: Qian ZQ, Liu T, Liu YY, Briesewitz R, Barrios AM, Jhiang SM, Pei DH
Publisher: American Chemical Society
Publication year: 2013
Volume number: 8
Issue number: 2
Start page: 423
End page: 431
Number of pages: 9
ISSN: 1554-8929
Languages: English-Great Britain (EN-GB)


Abstract

Cyclic peptides hold great potential as therapeutic agents and research tools, but their broad application has been limited by poor membrane permeability. Here, we report a potentially general approach for intracellular delivery of cyclic peptides. Short peptide motifs rich in arginine and hydrophobic residues (e.g., F Phi RRRR, where Phi is L-2-naphthylalanine), when embedded into small- to medium-sized cyclic peptides (7-13 amino acids), bound to the plasma membrane of mammalian cultured cells and were subsequently internalized by the cells. Confocal microscopy and a newly developed peptide internalization assay demonstrated that cyclic peptides containing these transporter motifs were translocated into the cytoplasm and nucleus at efficiencies 2-5-fold higher than that of nonaarginine (R-9). Furthermore, incorporation of the F Phi RRRR motif into a cyclic peptide containing a phosphocoumaryl aminopropionic acid (pCAP) residue generated a cell permeable, fluorogenic probe for detecting intracellular protein tyrosine phosphatase activities.


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Last updated on 2019-23-08 at 11:15