Computational design of a β-peptide that targets transmembrane helices

Scott J. Shandler, Ivan V. Korendovych, David T. Moore, Kathryn B. Smith-Dupont, Craig N. Streu, Rustem I. Litvinov, Paul C. Billings, Feng Gai, Joel S. Bennett, William F. Degrado

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


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 languageEnglish (US)
Pages (from-to)12378-12381
Number of pages4
JournalJournal of the American Chemical Society
Issue number32
StatePublished - Aug 17 2011
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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