4.3 Article

Proteomic exploration of soft and hard biocorona onto PEGylated multiwalled carbon nanotubes

Journal

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Volume 68, Issue 5, Pages 1003-1013

Publisher

WILEY
DOI: 10.1002/bab.2020

Keywords

biocompatibility; drug delivery; human plasma; mass spectrometry; PEGylated carbon nanotube; protein-corona

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This article discusses the potential application of carbon nanotubes in drug delivery systems, focusing on the characterization of protein corona as a crucial aspect in controlling the toxicity and cell targeting capabilities of nanotubes. The use of polyethylene glycol (PEG) to functionalize multiwalled carbon nanotubes (MWCNTs) and the subsequent incubation in human plasma to create the biocorona were key methods employed in the study. Analysis of the components of the biocorona was conducted through proteomic fingerprinting using methods like SDS-PAGE, 2D-PAGE separation, and mass spectrometry.
In nanomedicine, carbon nanotubes (CNTs) are considered potential candidates as drug delivery systems. The absorption of proteins onto CNTs, after their administration in physiological environment, forms the protein corona or biocorona, which is able to influence their biological properties and biocompatibility. For this reason, characterization of protein corona is a crucial aspect in the research to control CNTs toxicity and capability to target cells. Multiwalled carbon nanotubes (MWCNTs) were functionalized with polyethylene glycol (PEG), chosen considering its well-known biocompatibility, and then incubated in human plasma to create the biocorona. Plasma proteins, which bound around PEGylated CNTs, were detached using five different solutions, grouped into native and denaturant buffers, and used to characterize the two components of biocorona. The proteomic fingerprinting of biocorona was performed by SDS-PAGE and 2D-PAGE separation and mass spectrometry analysis. Native eluents were able to capture proteins of soft corona, characterized by complex secondary structures, and formed by both beta-sheet and alpha-helices domains. Denaturant buffers have eluted many proteins with a high percentage of the alpha-helix structure that could be involved in specific interactions responsible for the formation of hard corona.

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