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胶原模拟肽盘通过疏水相互作用促进多种天然蛋白质纤维的组装。

Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions.

作者信息

McGuinness Kenneth, Nanda Vikas

机构信息

Center for Advanced Biotechnology and Medicine, Rutgers University, 679 Hoes Lane West, Piscataway, NJ 08854, USA.

出版信息

Org Biomol Chem. 2017 Jul 19;15(28):5893-5898. doi: 10.1039/c7ob01073g.

DOI:10.1039/c7ob01073g
PMID:28678287
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6697174/
Abstract

Collagen mimetic peptides that alone formed two-dimensional nanoscale discs driven by hydrophobic interactions were shown in electron microscopy studies to also co-assemble with natural fibrous proteins to produce discs-on-a-string (DoS) nanostructures. In most cases, peptide discs also facilitated bundling of the protein fibers. This provides insight into how synthetic and natural proteins may be combined to develop multicomponent, multi-dimensional architectures at the nanoscale.

摘要

在电子显微镜研究中显示,仅通过疏水相互作用就能形成二维纳米级圆盘的胶原模拟肽,也能与天然纤维蛋白共同组装,产生串上圆盘(DoS)纳米结构。在大多数情况下,肽圆盘还促进了蛋白质纤维的成束。这为如何将合成蛋白和天然蛋白结合起来以开发纳米级的多组分、多维结构提供了见解。

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本文引用的文献

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Advances in the design and higher-order assembly of collagen mimetic peptides for regenerative medicine.用于再生医学的胶原模拟肽的设计与高阶组装进展。
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Organization and function of the 3D genome.三维基因组的组织与功能。
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Two-Dimensional Peptide and Protein Assemblies.二维肽和蛋白质组装体
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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.全长人α-突触核蛋白致病原纤维的固态核磁共振结构
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Morphological diversity and polymorphism of self-assembling collagen peptides controlled by length of hydrophobic domains.由疏水结构域长度控制的自组装胶原肽的形态多样性和多态性。
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