Abstract
The stereochemical effects of the hydrocarbon crosslink on the conformation and cellular uptake of i,i+4 stapled peptides were studied. Compared to its S,S-configurated counterpart, the crosslink bearing the R,R-configuration provided a significantly diminished helix stabilizing effect and conferred less efficient cellular uptake on the stapled peptides. These results suggest that the vesicular trafficking pathway employed by cells to take up stapled peptides is sensitive to the extent of helical character in the peptide, with greater helicity conferring increased cellular uptake.
Original language | English |
---|---|
Pages (from-to) | 2533-2536 |
Number of pages | 4 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 19 |
Issue number | 9 |
DOIs | |
State | Published - 1 May 2009 |
Keywords
- α-Helix
- Cellular uptake mechanism
- Helicity
- Stapled peptides
- Stereochemical effects