期刊
NATURE NANOTECHNOLOGY
卷 6, 期 8, 页码 469-479出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NNANO.2011.102
关键词
-
资金
- St John's College, Cambridge
- Office of Naval Research
- National Science Foundation
- Army Research Office
- Air Force Office of Scientific Research
- MRC [MC_G1000734] Funding Source: UKRI
- Medical Research Council [MC_G1000734] Funding Source: researchfish
Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed from many different peptides and proteins. Although these structures have an important role in neurodegenerative disorders, amyloid materials have also been exploited for functional purposes by organisms ranging from bacteria to mammals. Here we review the functional and pathological roles of amyloid materials and discuss how they can be linked back to their nanoscale origins in the structure and nanomechanics of these materials. We focus on insights both from experiments and simulations, and discuss how comparisons between functional protein filaments and structures that are assembled abnormally can shed light on the fundamental material selection criteria that lead to evolutionary bias in multiscale material design in nature.
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