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Interaction of gold and silver nanoparticles with human plasma: Analysis of protein corona reveals specific binding patterns. | LitMetric

Interaction of gold and silver nanoparticles with human plasma: Analysis of protein corona reveals specific binding patterns.

Colloids Surf B Biointerfaces

Key Laboratory for Biological Effects of Nanomaterials and Nanosafety of Chinese Academy of Sciences, Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing, 100190, P.R. China; University of Chinese Academy of Sciences, Beijing, 100049, P.R. China. Electronic address:

Published: April 2017

Determining how nanomaterials interact with plasma will assist in understanding their effects on the biological system. This work presents a systematic study of the protein corona formed from human plasma on 20nm silver and gold nanoparticles with three different surface modifications, including positive and negative surface charges. The results show that all nanoparticles, even those with positive surface modifications, acquire negative charges after interacting with plasma. Approximately 300 proteins are identified on the coronas, while 99 are commonly found on each nanomaterial. The 20 most abundant proteins account for over 80% of the total proteins abundance. Remarkably, the surface charge and core of the nanoparticles, as well as the isoelectric point of the plasma proteins, are found to play significant roles in determining the nanoparticle coronas. Albumin and globulins are present at levels of less than 2% on these nanoparticle coronas. Fibrinogen, which presents in the plasma but not in the serum, preferably binds to negatively charged gold nanoparticles. These observations demonstrate the specific plasma protein binding pattern of silver and gold nanoparticles, as well as the importance of the surface charge and core in determining the protein corona compositions. The potential downstream biological impacts of the corona proteins were also investigated.

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Source
http://dx.doi.org/10.1016/j.colsurfb.2017.01.037DOI Listing

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