Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1366695 | Bioorganic & Medicinal Chemistry Letters | 2007 | 4 Pages |
Cell penetrating peptides (CPP) displaying a type II polyproline helix backbone of different length and amphiphilic character were synthesized and their cellular uptake was compared. The longer CPP sequence, P14LRR, displayed a 7- to 12-fold higher uptake in MCF-7 cells as compared to its shorter counterpart, P11LRR, and a 35-fold higher uptake as compared to Tatp. These results demonstrate that an increased number of cationic and hydrophobic residues can strongly influence the extent of cellular internalization. Mechanistic investigations suggest internalization via a receptor independent endocytotic pathway with these agents.
Graphical abstractInvestigations of length effects and mechanism of cell penetrating peptides displaying a rigid polyproline helix backbone are reported.Figure optionsDownload full-size imageDownload as PowerPoint slide