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

Computational design of a β-peptide that targets transmembrane helices.

Author information

1
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

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(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.

PMID:
21780757
PMCID:
PMC3155016
DOI:
10.1021/ja204215f
[Indexed for MEDLINE]
Free PMC Article

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