期刊
JOURNAL OF MATERIALS CHEMISTRY B
卷 1, 期 5, 页码 668-675出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c2tb00105e
关键词
-
资金
- National Natural Science Foundation of China [51125014, 51233003]
- Ministry of Science and Technology of China [2011CB606202]
- Fundamental Research Funds for the Central Universities [2012203020201]
Neurodegenerative diseases including Alzheimer's, Parkinson's, and type II diabetes are recognized to be related to proteins misfolding into amyloid fibrils and other aggregates with a beta-sheet conformation. Herein, self-assembled peptide micro/nanoarchitectures were designed and prepared to mimic those aggregates. A short beta-amyloid peptide derivative with a diphenylalanine moiety was synthesized, which could self-assemble into nanofibers via beta-sheet conformation in an aqueous solution with a concentration of 1 mg mL(-1) at pH about 8. By adjusting the pH to around 6.5, a peptide solution with a concentration of 15 mg mL(-1) could change to a supramolecular hydrogel. The influence of self-assembly conditions including peptide concentration, temperature, pressure, and self-assembly time were investigated in detail. It was found that the self-assembled nanofibers could further aggregate into catenulate microfibers in solution as well as layer-by-layer plaques in the hydrogel under particular conditions.
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