کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1366695 | 981600 | 2007 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Probing length effects and mechanism of cell penetrating agents mounted on a polyproline helix scaffold Probing length effects and mechanism of cell penetrating agents mounted on a polyproline helix scaffold](/preview/png/1366695.png)
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.
Investigations of length effects and mechanism of cell penetrating peptides displaying a rigid polyproline helix backbone are reported.Figure optionsDownload as PowerPoint slide
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 17, Issue 10, 15 May 2007, Pages 2765–2768