Computational design of a β-peptide that targets transmembrane helices

J Am Chem Soc. 2011 Aug 17;133(32):12378-81. doi: 10.1021/ja204215f. Epub 2011 Jul 22.


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(IIb)β(3). The designed peptide (β-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Computer-Aided Design
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Platelet Glycoprotein GPIIb-IIIa Complex / metabolism*
  • Protein Binding
  • Protein Structure, Secondary


  • Peptides
  • Platelet Glycoprotein GPIIb-IIIa Complex