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通过金纳米粒子抑制短两亲肽的β-折叠(淀粉样纤维)形成实现高效基因转染。

Efficient Gene Transfection through Inhibition of β-Sheet (Amyloid Fiber) Formation of a Short Amphiphilic Peptide by Gold Nanoparticles.

机构信息

Institute for Organic Chemistry, University of Duisburg-Essen, 45117, Essen, Germany.

Institute for Biology, University of Duisburg-Essen, 45117, Essen, Germany.

出版信息

Angew Chem Int Ed Engl. 2017 Jul 3;56(28):8083-8088. doi: 10.1002/anie.201700713. Epub 2017 Apr 10.

Abstract

The effect of citrate-stabilized gold nanoparticles (AuNPs) on the secondary structure of an artificial β-sheet-forming cationic peptide has been studied. The AuNPs inhibited β-sheet formation and led to fragmented fibrils and spherical oligomers with assembled AuNPs on their surface. Besides this structural change, the functional properties of the peptide are also different. Whereas the peptide was unable to act as a vector for gene delivery, formation of a complex with AuNPs allowed successful gene delivery into cells.

摘要

研究了柠檬酸稳定的金纳米粒子(AuNPs)对人工β-折叠形成阳离子肽的二级结构的影响。AuNPs 抑制β-折叠形成,并导致纤维的碎片化和表面组装有 AuNPs 的球形寡聚物。除了这种结构变化外,肽的功能特性也不同。虽然该肽不能作为基因传递的载体,但与 AuNPs 形成复合物可成功将基因递送至细胞中。

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