期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 118, 期 7, 页码 1765-1774出版社
AMER CHEMICAL SOC
DOI: 10.1021/jp409988n
关键词
-
资金
- Cyprus Research Promotion Foundation [ANAVATHMISI/0609/11]
- European Regional Development Fund
- University of Cyprus
- Greek General Secretariat for Research and Technology grant Herakleitos II [10.74.11.01]
- CRISP consortium
- European Commission [283745]
The self-assembly of short peptides into fibrous nanostructures (such as fibrils and tubes) has recently become the subject of intense theoretical and experimental scrutiny, as such assemblies are promising candidates for nano-biotechnological applications. The sequences of natural fibrous proteins may provide a rich source of inspiration for the design of such short self-assembling peptides. We describe the self-assembly of the aspartate-rich undecapeptide (NH3+-LSGSDSDTL-TV-NH2), a sequence derived from the shaft of the adenovirus fiber. We demonstrate that the peptide assembles experimentally into amyloid-type fibrils according to widely accepted diagnostic criteria. In addition, we investigate an aqueous solution of undecapeptides by molecular dynamics simulations with an implicit (GB) solvent model. The peptides are frequently arranged in intermolecular beta-sheets, in line with their amyloidogenic propensity. On the basis of both experimental and theoretical insights, we suggest possible structural models of the fibrils and their potential use as scaffolds for templating of inorganic materials.
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