Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore

被引：6

作者：

Coglitore, Diego ^{[1
]}

Coulon, Pierre Eugene ^{[2
]}

Janot, Jean-Marc ^{[1
]}

Balme, Sebastien ^{[1
]}

机构：

[1] Univ Montpellier, Inst Europeen Membranes, CNRS, UMR5635,ENSCM, Pl Eugene Bataillon, F-34090 Montpellier, France

[2] Univ Paris Saclay, Ecole Polytech, Lab Solides Irradies, Route Saclay, F-91128 Palaiseau, France

来源：

MATERIALS | 2019年 / 12卷 / 21期

关键词：

protein corona; nanopore; single molecule; BOVINE SERUM-ALBUMIN; GOLD NANOPARTICLES; ADSORPTION; IDENTIFICATION; TRANSLOCATION; STABILITY; DYNAMICS; BEHAVIOR; BINDING; CATH;

D O I：

10.3390/ma12213524

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Protein adsorption at the liquid-solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparticles and the colloidal properties. The protein panel was chosen from different structural categories (mainly-alpha, mainly-beta or mix-alpha beta). The result shows that the colloidal stability with salt addition does not depend on the structural category. Conversely, using the single nanopore technique, we show that the mainly-alpha proteins form a smaller corona than the mainly-beta proteins. We assign these observations to the lower internal energy of alpha-helices, making them more prone to form a homogeneous corona layer.

引用

页数：11

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