The nanoparticle–protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century

Lynch, Iseult; Cedervall, Tommy; Lundqvist, Martin; Cabaleiro-Lago, Celia; Linse, Sara; Dawson, Kenneth A.

doi:10.1016/j.cis.2007.04.021

Cited by 659 publications

(556 citation statements)

References 24 publications

Supporting

Mentioning

541

Contrasting

Unclassified

Order By: Relevance

“…Thus, whilst nanoparticles potentially change the conformation of the cell membrane, resulting in a disruption of cellular processes and membrane integrity [23,24], most interactions with the cell membrane do not cause any membrane disruption or extraction of the protein from the plasmalemma, as previously observed in the case of cyclodextrins [25]. This was confirmed by Western blot analysis of the cells and their supernatant.…”

Section: Discussionsupporting

confidence: 66%

Nanoparticles attenuate P-glycoprotein/MDR1 function in A549 human alveolar epithelial cells

Salomon

Ehrhardt

2011

European Journal of Pharmaceutics and Biopharmaceutics

View full text Add to dashboard Cite

P-glycoprotein/MDR1 (P-gp) is a well characterised membrane transporter relevant in drug disposition and multi-drug resistance. In this study, we aimed to investigate in how far nanoparticulates impair the function of the P-gp transport system, and which particle properties govern these interactions.Expression and function of P-gp was confirmed in A549 cell monolayers. Rhodamine 123 (Rh123) release studies were carried out in the presence of known inhibitors of Pgp function (i.e., cyclosporine A and verapamil), under ATP depletion (NaN 3 /DOG) and after acute exposure to nanoparticles (NPs) with different surface modifications, ζ-potentials and sizes (plain, carboxylated, and amine-and sulphate-modified). The cytotoxic potential of NPs on A549 monolayers was evaluated by MTT assay. The effects on P-gp protein level, after incubation with NPs, were investigated by Western blot analysis of A549 cell lysate and supernatant. Cellular retention of Rh123 was significantly (P < 0.05) increased in the presence of carboxylated (100 nm), amine-and sulphate-modified NPs. A slight, but not significant, decrease in Rh123 release was also observed for plain latex and carboxylated (500 nm)NPs. The MTT assay demonstrated that most NPs caused only marginal levels of cytotoxicity (78-88% cell viability); the positively charged amine-NPs, however, were considerably more cytotoxic. Western blot showed that NPs did not cause any cell membrane disruption.Our findings suggest that nanomaterials can attenuate membrane transporter function depending on their size and surface properties and hence, might influence disposition of xenobiotics as well as endogenous substrates.

show abstract

Section: Discussionsupporting

confidence: 66%

Nanoparticles attenuate P-glycoprotein/MDR1 function in A549 human alveolar epithelial cells

Salomon

Ehrhardt

2011

European Journal of Pharmaceutics and Biopharmaceutics

View full text Add to dashboard Cite

show abstract

“…The small sizes of nanoparticles present a relatively large surface curvature that facilitates attachment of proteins (5). Furthermore, the degree of the structural perturbation that proteins undergo in response to their interaction with particular nanoparticles varies across protein species.…”

Section: Introductionmentioning

confidence: 99%

Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

et al. 2013

View full text Add to dashboard Cite

Gold nanoparticles show a lot of promise as potential agents for drug delivery and disease diagnosis. Because of this, it is important that the interaction between gold nanoparticles and biomolecules be well characterized to avoid undesirable consequences. In this study, gold nanoparticles were synthesized by the reduction of gold salt by sodium borohydride in the presence of cysteine as the capping agent. The physical features of the nanoparticles were analyzed using Ultraviolet-Visible spectrophotometry and transmission electron microscopy. The interaction between gold nanoparticles and the following proteins: bovine serum albumin, citrate synthase, malate dehydrogenase, and human heat shock protein 70 was investigated by UV-Vis spectrophotometry. The stability of the proteins against heat stress was assessed by monitoring their aggregation at 48 8C, either in the presence or absence of gold nanoparticles. The gold nanoparticles were capable of suppressing the heat-induced aggregation of the proteins. Furthermore, apart from possessing independent protein-aggregation suppression function, the AuNPs also augmented the chaperone function of human heat shock protein 70. Findings from this study demonstrate that cyteinecoated gold nanoparticles exhibit chaperone-like activity and have the capability to stabilize proteins to which they may be conjugated. V C 2013 IUBMB Life, 65(5): 454-461, 2013.

show abstract

“…The Dawson group has pioneered structure-property-relationships in protein coronas during the last few years using plasma proteins [3][4][5][6]. However, there is general consensus in nanotoxicology that inhalation represents the most relevant route of exposure [7].…”

Section: Introductionmentioning

confidence: 99%

Interaction of metal oxide nanoparticles with lung surfactant protein A

Schulze

Schaefer

Ruge

et al. 2011

European Journal of Pharmaceutics and Biopharmaceutics

View full text Add to dashboard Cite

show abstract

The nanoparticle–protein complex as a biological entity; a complex fluids and surface science challenge for the 21st century

Cited by 659 publications

References 24 publications

Nanoparticles attenuate P-glycoprotein/MDR1 function in A549 human alveolar epithelial cells

Nanoparticles attenuate P-glycoprotein/MDR1 function in A549 human alveolar epithelial cells

Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress

Interaction of metal oxide nanoparticles with lung surfactant protein A

Contact Info

Product

Resources

About