2014
DOI: 10.1016/j.colsurfb.2013.08.047
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Conformational changes in human plasma proteins induced by metal oxide nanoparticles

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Cited by 55 publications
(64 citation statements)
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“…In contrast, a slight red region-shift on the emission band of the globulins suggests an adsorption of these proteins exclusively on the MIL-100(Fe) surface, which may exhibit a more unfolded conformation with more exposed tryptophan residues. [ 58 ] Interestingly, transferrin, an iron-binding blood plasma glycoprotein belonging to the globulin family, could be the responsible of this slight conformational change, only visible at high NP concentration (100 µg mL −1 ), as a consequence of their interaction with iron. Conversely, the heparin-coated MIL-100(Fe) NPs did not show any signifi cant shift, in agreement with the absence of conformational changes of globulins.…”
Section: Uptake By Macrophages Cell Viability Ros Production and Cmentioning
confidence: 99%
See 1 more Smart Citation
“…In contrast, a slight red region-shift on the emission band of the globulins suggests an adsorption of these proteins exclusively on the MIL-100(Fe) surface, which may exhibit a more unfolded conformation with more exposed tryptophan residues. [ 58 ] Interestingly, transferrin, an iron-binding blood plasma glycoprotein belonging to the globulin family, could be the responsible of this slight conformational change, only visible at high NP concentration (100 µg mL −1 ), as a consequence of their interaction with iron. Conversely, the heparin-coated MIL-100(Fe) NPs did not show any signifi cant shift, in agreement with the absence of conformational changes of globulins.…”
Section: Uptake By Macrophages Cell Viability Ros Production and Cmentioning
confidence: 99%
“…As recently shown by some of us, NPs can induce conformational changes on proteins, altering also their function. [ 58 ] To gain further understanding, we investigated if upon adsorption of the main plasma proteins (fi brinogen, albumin, and globulins) on both the uncoated and heparin-coated NPs, the proteins could undergo conformational changes. Thus, both NPs were incubated in presence of increasing concentration of each protein fraction, analyzing the conformational changes by using fl uorescence spectroscopy (see Experimental Section).…”
Section: Uptake By Macrophages Cell Viability Ros Production and Cmentioning
confidence: 99%
“…The Np size was determined by high-resolution transmission electron microscopy, and all of the Nps were uncoated and free of surfactant. The transmission electron microscopy images and dynamic light scattering characterization have been described previously 26 and they are shown in Figure S1. The Nps were resuspended in milli-Q water at 10 mg/mL and, after sonication, 10% fetal bovine serum was added to reduce the aggregation of the Nps.…”
Section: Introductionmentioning
confidence: 99%
“…Also, whether the particles are agglomerated or not on the biological fluids [33,101] could strongly modify their uptake. Moreover, nanoparticles can induce conformational changes in proteins, affecting their physiological function [147]. Thus, in vivo fate of nanostructures and the biological responses could be altered when compared with in vitro studies.…”
Section: Protein Coronamentioning
confidence: 99%
“…Possible nanostructure-cellular interactions may induce cytotoxicity and other physio-logical outcomes to GI tract. For example, oxidative stress, inflammation and immune responses (phagocytosis, complement activation and recruitment of inflammatory cells) [187], mitochondrial perturbation, ''corona'' formation (please see ''Protein corona'' section), protein denaturation [147], DNA damage and cell death [33,81,97]. Although some of these responses could be beneficial for some purposes, such as the activation of specific immune responses by nanostructures carrying antigens on vaccines [128,168], some of those could have harmful effects.…”
Section: Nanotoxicity Assessment In Gi Tractmentioning
confidence: 99%