Ontology highlight
ABSTRACT:
SUBMITTER: Shandler SJ
PROVIDER: S-EPMC3155016 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature
Shandler Scott J SJ Korendovych Ivan V IV Moore David T DT Smith-Dupont Kathryn B KB Streu Craig N CN Litvinov Rustem I RI Billings Paul C PC Gai Feng F Bennett Joel S JS DeGrado William F WF
Journal of the American Chemical Society 20110722 32
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-CH ...[more]