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 journalArticle

38 Scopus citations

Abstract

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
Volume133
Issue number32
DOIs
StatePublished - Aug 17 2011

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Shandler, S. J., Korendovych, I. V., Moore, D. T., Smith-Dupont, K. B., Streu, C. N., Litvinov, R. I., Billings, P. C., Gai, F., Bennett, J. S., & Degrado, W. F. (2011). Computational design of a β-peptide that targets transmembrane helices. Journal of the American Chemical Society, 133(32), 12378-12381. https://doi.org/10.1021/ja204215f