Coassembly of amphiphiles with opposite peptide polarities into nanofibers
Coassembly of amphiphiles with opposite peptide polarities into nanofibers
复制标题
DOI：
10.1021/ja044863u
复制
发表时间：
2005-02-02
影响因子：
15
通讯作者：
Stupp, SI
中科院分区：
文献类型：
--
作者：
Behanna, HA;Donners, JJJM;Stupp, SI
描述了具有游离 N 末端的“反向”肽两亲物 (PAS) 的设计、合成和表征。使用脂肪酸尾修饰的非天然氨基酸可以合成此类新型 PA 分子。这些分子与含有游离 C 末端的互补分子混合会产生共组装结构，如圆二色性和 NOE/NMR 光谱所证明的那样。与仅由一种 PA 分子组成的组件相比，这些组件表现出不同寻常的热稳定性。此类反向 PAS 使得利用游离 N 端肽序列创建具有生物学意义的组装体成为可能，而这些组装体以前是无法获得的，包括源自噬菌体展示方法的序列。
The design, synthesis, and characterization of "reverse" peptide amphiphiles (PAS) with free N-termini is described. Use of an unnatural amino acid modified with a fatty acid tail allows for the synthesis of this new class of PA molecules. The mixing of these molecules with complementary ones containing a free C-terminus results in coassembled structures, as demonstrated by circular dichroism and NOE/NMR spectroscopy. These assemblies show unusual thermal stability when compared to assemblies composed of only one type of PA molecule. This class of reverse PAS has made it possible to create biologically significant assemblies with free N-terminal peptide sequences, which were previously inaccessible, including those derived from phage display methodologies.