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金纳米粒子上接枝蛋白质的原子结构细节。

Atomic structural details of a protein grafted onto gold nanoparticles.

机构信息

Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 3, 50019, Sesto Fiorentino, Italy.

Magnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.

出版信息

Sci Rep. 2017 Dec 20;7(1):17934. doi: 10.1038/s41598-017-18109-z.

Abstract

The development of a methodology for the structural characterization at atomic detail of proteins conjugated to nanoparticles would be a breakthrough in nanotechnology. Solution and solid-state NMR spectroscopies are currently used to investigate molecules and peptides grafted onto nanoparticles, but the strategies used so far fall short in the application to proteins, which represent a thrilling development in theranostics. We here demonstrate the feasibility of highly-resolved multidimensional heteronuclear spectra of a large protein assembly conjugated to PEGylated gold nanoparticles. The spectra have been obtained by direct proton detection under fast MAS and allow for both a fast fingerprinting for the assessment of the preservation of the native fold and for resonance assignment. We thus demonstrate that the structural characterization and the application of the structure-based methodologies to proteins bound to gold nanoparticles is feasible and potentially extensible to other hybrid protein-nanomaterials.

摘要

开发一种用于对与纳米粒子结合的蛋白质进行原子细节结构描述的方法将是纳米技术的一个突破。目前,溶液和固态 NMR 光谱学被用于研究接枝到纳米粒子上的分子和肽,但迄今为止使用的策略在应用于蛋白质方面存在不足,而蛋白质在治疗学中是一个令人激动的发展。我们在这里证明了与聚乙二醇化金纳米粒子结合的大蛋白质组装体的高分辨多维异核光谱的可行性。这些光谱是通过快速 MAS 下的直接质子检测获得的,不仅可以快速进行指纹分析以评估天然折叠的保留情况,还可以进行共振分配。因此,我们证明了对与金纳米粒子结合的蛋白质进行结构表征和基于结构的方法的应用是可行的,并且可能扩展到其他混合蛋白质-纳米材料。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d0d/5738368/2ab93c103c07/41598_2017_18109_Fig1_HTML.jpg

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