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- W1971831337 endingPage "2768" @default.
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- W1971831337 abstract "Investigations of length effects and mechanism of cell penetrating peptides displaying a rigid polyproline helix backbone are reported. 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." @default.
- W1971831337 created "2016-06-24" @default.
- W1971831337 creator A5039949898 @default.
- W1971831337 creator A5043317624 @default.
- W1971831337 date "2007-05-01" @default.
- W1971831337 modified "2023-09-27" @default.
- W1971831337 title "Probing length effects and mechanism of cell penetrating agents mounted on a polyproline helix scaffold" @default.
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- W1971831337 doi "https://doi.org/10.1016/j.bmcl.2007.02.077" @default.
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