Nanoparticle-Templated Self-Assembly of Viral Capsids Probed by Time-Resolved Absorbance Spectroscopy and X-Ray Scattering

被引：7

作者：

Burke, Andrew ^{[1
]}

Chevreuil, Maelenn ^{[1
]}

Paris, Alisier ^{[1
]}

de La Grange, Vanessa ^{[1
]}

Goldmann, Claire ^{[1
]}

Perez, Javier ^{[2
]}

Constantin, Doru ^{[1
]}

Tresset, Guillaume ^{[1
]}

机构：

[1] Univ Paris Saclay, Univ Paris Sud, CNRS, Lab Phys Solides, F-91405 Orsay, France

[2] SOLEIL Synchrotron, F-91192 Gif Sur Yvette, France

来源：

PHYSICAL REVIEW APPLIED | 2018年 / 10卷 / 05期

关键词：

CHLOROTIC-MOTTLE-VIRUS; GOLD NANOPARTICLES; MONODISPERSE GOLD; PATHWAY; PROTEIN; KINETICS; PARTICLES; STABILITY; EFFICIENT; DEPENDS;

D O I：

10.1103/PhysRevApplied.10.054065

中图分类号：

O59 [应用物理学];

学科分类号：

摘要：

Viral capsid proteins have the remarkable ability to self-assemble around a cargo core, whether their genome, a polyelectrolyte or an inorganic nanoparticle. Although the equilibrium properties of gold nanoparticles encapsulated in viral capsids have been broadly investigated, little is known about the kinetic pathways leading to their assembly. Through the combination of time-resolved absorbance spectroscopy and small-angle x-ray scattering, we elucidate a three-step mechanism with timescales ranging from hundred milliseconds to hours. By modeling the scattering intensities, we deduce the average structure and the time evolution of transient, amorphous aggregates held in a matrix of capsid proteins. The biocompatibility of metal nanoparticles induced by adsorbed proteins is of great importance for their use in biomedicine, and the reported results will help better understand the formation process.

引用

页数：10

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