期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 64, 期 -, 页码 106-115出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2021.05.004
关键词
Amyloid; Amyloidogenic peptides and proteins; a-Synuclein; Superoxide dismutase 1 (SOD1); aB crystallin; Human; prion protein hPrP; Amyloid oligomers; Fibrils; Model peptide systems; Stabilized 0-hairpins; Macrocyclic; 0-hairpin peptides; X-ray crystallography; NMR; CryoEM; Molecular; modeling
资金
- National Institutes of Health [GM097562, AG062296]
- National Science Foundation [CHE-1808096]
- University of California, Irvine
This article summarizes recent advances in utilizing peptide model systems to investigate and understand the structures, biological properties, and biophysical properties of amyloid oligomers.
The assembly of amyloidogenic peptides and proteins, such as the 0-amyloid peptide, a-synuclein, huntingtin, tau, and islet amyloid polypeptide, into amyloid fibrils and oligomers is directly linked to amyloid diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases, frontotemporal dementias, and type II diabetes. Although amyloid oligomers have emerged as especially important in amyloid diseases, high-resolution structures of the oligomers formed by fulllength amyloidogenic peptides and proteins have remained elusive. Investigations of oligomers assembled from fragments or stabilized 0-hairpin segments of amyloidogenic peptides and proteins have allowed investigators to illuminate some of the structural, biophysical, and biological properties of amyloid oligomers. Here, we summarize recent advances in the application of these peptide model systems to investigate and understand the structures, biological properties, and biophysical properties of amyloid oligomers.
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