Interactions of blood proteins with poly(isobutylcyanoacrylate) nanoparticles decorated with a polysaccharidic brush

Abstract

The aim of this work was to examine the in vitro interactions of core-shell poly(isobutylcyanoacrylate)-polysaccharide nanoparticles (NP) with blood proteins. The particles were prepared by initiating the emulsion polymerization of isobutylcyanoacrylate (IBCA) in the presence of dextran 71 or 15 kDa, heparin, a blend of dextran 71 and heparin, or dextran sulphate in aqueous medium at pH 1. The mechanisms of polymerisation were redox radical (Rad) or anionic (An), resulting in differences in the spatial arrangement of the polysaccharide chains at the NP surface, i.e. "loops" and "trains" by anionic polymerization, "brush" by radical polymerization. Surface composition of NPs was determined by X-ray photo-electron spectroscopy (XPS) and surface charge by zeta potential measurements. In the presence of citrated blood plasma, efficacy of the steric repulsive effect of the NP dextran shell towards protein adsorption decreased in the order: Dex71-Rad > Dex15-Rad > Dex71-AnDex15-An. Dextran-coated NPs adsorbed ApoA-I and fibrinogen from plasma. Concerning activation of complement in serum, the effect was sharp: Dex71-Rad was a very low activator whereas Dex15-An, Dex15-Rad and Dex71-An were strong activators. In citrated plasma, the steric repulsive effects of Hep-Rad and Dex-Hep-Rad NPs were similar to Dex71-An, and Dex-Sulph-Rad NPs adsorbed twice more proteins than Hep-Rad. Hep-Rad, Dex-Hep-Rad and Dex-Sulph-Rad NPs adsorbed IgG and fibrinogen. Complement was not activated in serum in the presence of Hep-Rad and Dex-Hep-Rad and a slight adsorption of C3 was noted. C3 was completely adsorbed on Dex-Sulph-Rad. The exquisite sensitivity of blood proteins to differences in the nature and outermost structure of the polysaccharides-coated NPs is highlighted by the present results.

The Interactions between Blood and Polymeric Nanoparticles Depend on the Nature and Structure of the Hydrogel Covering the Surface

“…ApoA-1 was found to be the main protein adsorbed on both types of NP bearing the longer dextran, whereas a fragment of fibrinogen was found as the main species adsorbed on both types of NPs bearing the shorter dextran. More details can be found in Labarre et al [32]. ApoA-1 was also found as second or third protein adsorbed on the surface of all NPs, in accordance to the results obtained by Cornelius et al [33].…”

Development of a Novel Vaccine Delivery System Based on Gantrez Nanoparticles

“…This technique was performed by a modification of a protocol previously described by Labarre et al 18 .…”

Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

“…A central methodological problem is to separate free protein from protein bound to nanoparticles, ideally employing nonperturbing methods that do not disrupt the protein-particle complex or induce additional protein binding. The preferred method to-date has been centrifugation, identifying the major serum proteins albumin, IgG and fibrinogen as being associated with a wide range of particles of seemingly disparate molecular composition (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18). Due to its high abundance, albumin is almost always observed on particles and may be retrieved even if it has relatively low affinity.…”