Equilibrium binding of isolated and in-plasma high-density lipoproteins (HDLs) to polystyrene nanoparticles
- PDF / 1,060,842 Bytes
- 9 Pages / 547.087 x 737.008 pts Page_size
- 56 Downloads / 178 Views
RESEARCH PAPER
Equilibrium binding of isolated and in-plasma high-density lipoproteins (HDLs) to polystyrene nanoparticles Uche C. Anozie & Kevin J. Quigley & Aaron Prescott & Steven M. Abel & Paul Dalhaimer
Received: 20 March 2020 / Accepted: 10 July 2020 # Springer Nature B.V. 2020
Abstract It is hypothesized that plasma proteins bind nanoparticles in vivo as they do in vitro, forming a protein corona. The resulting decorated nanoparticle surface could potentially alter nanoparticle pharmacokinetics, efficacy, and toxicity in vivo. A subset of the in vitro corona are high-density lipoproteins (HDLs). Since HDLs vary in patients based on diet, weight, and genetics, it is crucial to determine the affinity of HDLs for nanoparticles to generate a predictive model, which would provide information on the extent of HDL decoration on nanoparticles in the blood. Experiments that determined equilibrium affinities of HDLs for nanoparticles utilized isolated HDLs or HDL structural protein components such as ApoA-I. Thus, the effects of whole plasma on HDL-nanoparticle equilibrium binding are unclear. It is possible that competition from other plasma proteins for the nanoparticle surface could drastically change the affinity of HDLs for nanoparticles both in vitro and in vivo. Here, we determined effective equi-
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s11051-020-04953-0) contains supplementary material, which is available to authorized users. U. C. Anozie : K. J. Quigley : A. Prescott : S. M. Abel : P. Dalhaimer Department of Chemical and Biomolecular Engineering, University of Tennessee, 426 Dougherty Engineering Building, 1512 Middle Drive, Knoxville, TN 37996, USA P. Dalhaimer (*) Department of Biochemistry, Cellular, and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA e-mail: [email protected]
librium binding constants of Kdeff = 3.1 ± 0.7 μM, 1.2 ± 0.4 μM, and 2.0 ± 0.4 μM for polystyrene (PS), PSCOOH, and PS-NH2 nanospheres for ApoA-I, the main structural component of HDLs in whole mouse plasma. In comparison, binding constants were Kd = 400 nM, 900 nM, and 25 nM for PS, PS-COOH, and PS-NH2 nanospheres and HDLs isolated from mouse plasma. We utilized a binding model that is characterized by a nanoparticle with multiple identical and independent binding sites for HDLs. Our data show that HDL binding to nanoparticles could play a significant role in nanoparticle behavior in the vasculature of mammals. Keywords High-density lipoproteins . Nanobiomedicine . Nanoparticles . Protein corona . Binding affinity
Introduction Lipoproteins constitute a major component of the biomolecular corona, which associates with nanoparticles after exposure to plasma in vitro (Cedervall et al. 2007; Deng et al. 2009; Dobrovolskaia et al. 2009; Göppert and Müller 2005; Gossmann et al. 2015; Olbrich et al. 2004; Tenzer et al. 2013). High-density lipoproteins (HDLs) and low-density lipoproteins (LDLs) are two major classes of lipoproteins that have been found in the n
Data Loading...
