The structure of the cell-permeable h-helical amphipathic model peptide FLUOS-KLALKLALKA-LKAALKLA-NH 2 (I) was modified stepwise with respect to its helix parameters hydrophobicity, hydrophobic moment and hydrophilic face as well as molecular size and charge. Cellular uptake and membrane destabilizi
Cellular uptake of Aib-containing amphipathic helix peptide
✍ Scribed by Shun-ichi Wada; Hirokazu Tsuda; Terumi Okada; Hidehito Urata
- Book ID
- 113496073
- Publisher
- Elsevier Science
- Year
- 2011
- Tongue
- English
- Weight
- 378 KB
- Volume
- 21
- Category
- Article
- ISSN
- 0960-894X
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## Abstract The packing of peptide helices in crystals of the leucine‐rich decapeptide Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe provides an example of ladder‐like leucylleucyl interactions between neighboring molecules. The peptide molecule forms a helix with five 5→1 hydrogen bonds and two