期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 32, 页码 12378-12381出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja204215f
关键词
-
资金
- NIH [GM54616, GM60610, HL40387]
- NSF MRSEC
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1120901] Funding Source: National Science Foundation
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据