The design of β-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of β-peptides was designed to stably insert in TM orientations in phospholipid bilayers. Their secondary structures and orientation in the phospholipid bilayer was characterized using biophysical methods. Computational methods were then devised to design a β-peptide that targeted a TM helix of the integrin α IIbβ 3. The designed peptide (β-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.
|Original language||English (US)|
|Number of pages||4|
|Journal||Journal of the American Chemical Society|
|State||Published - Aug 17 2011|
ASJC Scopus subject areas
- Colloid and Surface Chemistry