Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 32, Pages 12378-12381Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja204215f
Keywords
-
Categories
Funding
- NIH [GM54616, GM60610, HL40387]
- NSF MRSEC
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1120901] Funding Source: National Science Foundation
Ask authors/readers for more resources
The design of beta-peptide foldamers targeting the transmembrane (TM) domains of complex natural membrane proteins has been a formidable challenge. A series of beta-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 beta-peptide that targeted a TM helix of the integrin alpha(IIb)beta(3). The designed peptide (beta-CHAMP) interacts with the isolated target TM domain of the protein and activates the intact integrin in vitro.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available