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Convergent synthesis and cellular uptake of multivalent cell penetrating peptides derived from Tat, Antp, pVEC, TP10 and SAP

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Eggimann Gabiela A. , Buschor Stefanie, Darbre Tamis, Reymond Jean-Louis,
Project Exploring Peptide Topologies in Search for New Drugs
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Original article (peer-reviewed)

Journal Org. Biomol. Chem.
Volume (Issue) 11(39)
Page(s) 6717 - 6733
Title of proceedings Org. Biomol. Chem.
DOI 10.1039/c3ob41023d

Open Access

Type of Open Access Publisher (Gold Open Access)


Cell penetrating peptides (CPP) are peptides of 10 to 30 residues derived from natural translocating pro- teins. Multivalency is known to enhance cellular uptake for the Tat peptide and closely related polycatio- nic sequences. To test whether multivalency effects on cellular uptake might also occur with other CPP types, we prepared multivalent versions of the strongly cationic Tat, the amphipathic sequences Antp, pVEC and TP10, and the polyproline helix SAP by convergent thioether ligation of the linear CPP onto multivalent scaffolds, and evaluated their uptake in HeLa and CHO cells, intracellular localization, cytotoxicity and hemolysis. While multivalency did not increase the cellular uptake of pVEC or SAP, multi- valency effects on uptake comparable to Tat were observed with TP10 and Antp, which are attributable to their polycationic nature. The efficient synthetic protocol for these divalent CPP and their localization in the cytoplasm suggest that CPP might be useful for application in cargo delivery into cells.