Issue 45, 2018

Protein denaturation caused by heat inactivation detrimentally affects biomolecular corona formation and cellular uptake

Abstract

Adsorption of blood proteins to the surface of nanocarriers is known to be the critical factor influencing cellular interactions and eventually determining the successful application of nanocarriers as drug carriers in vivo. There is an increasing number of reports summarizing large data sets of all identified corona proteins. However, to date our knowledge about the multiple mechanisms mediating interactions between proteins and nanocarriers is still limited. In this study, we investigate the influence of protein structure on the adsorption process and focus on the effect of heat inactivation of serum and plasma, which is a common cell culture procedure used to inactivate the complement system. As in general routine lab procedure, heat inactivation was performed at 56 °C for 30 min in order to denature heat labile proteins. When nanocarriers were exposed to native versus heat inactivated serum, we saw that the cellular uptake by macrophages was significantly affected. These results were then correlated with an altered corona composition that depended on the treatment of the protein source. In summary, we were able to prove that the protein structure is one of the key parameters determining protein corona formation.

Graphical abstract: Protein denaturation caused by heat inactivation detrimentally affects biomolecular corona formation and cellular uptake

Supplementary files

Article information

Article type
Paper
Submitted
12 sen 2018
Accepted
01 noy 2018
First published
01 noy 2018
This article is Open Access
Creative Commons BY license

Nanoscale, 2018,10, 21096-21105

Protein denaturation caused by heat inactivation detrimentally affects biomolecular corona formation and cellular uptake

J. Simon, J. Müller, A. Ghazaryan, S. Morsbach, V. Mailänder and K. Landfester, Nanoscale, 2018, 10, 21096 DOI: 10.1039/C8NR07424K

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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