Biocompatibility of mannan nanogel--safe interaction with plasma proteins.

Background: Self-assembled mannan nanogels are designed to provide a therapeutic or vaccine delivery platform based on the bioactive properties of mannan to target mannose receptor expressed on the surface of antigen-presenting cells, combined with the performance of nanogels as carriers of biologically active agents.

Methods: Proteins in the corona around mannan nanogel formed in human plasma were identified by mass spectrometry after size exclusion chromatography or centrifugation followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Structural changes and time dependent binding of human apolipoprotein A-I (apoA-I) and human serum albumin (HSA) to mannan nanogel were studied using intrinsic tryptophan fluorescence and circular dichroism spectroscopy.

Polystyrene nanoparticles affecting blood coagulation.

The association of nanoparticles (NPs) with blood coagulation proteins may influence the natural balance between pro- and anticoagulant pathways. We investigated whether polystyrene NPs, when added to human plasma, affected the generation of thrombin in plasma. Amine-modified NPs were found to decrease the thrombin formation due to binding of factors VII and IX to the NPs, which resulted in depletion of the respective protein in solution.

Structural changes in apolipoproteins bound to nanoparticles.

Nanoparticles are widely used in the pharmaceutical and food industries, but the consequences of exposure to the human body have not been thoroughly investigated. Apolipoprotein A-I (apoAI), the major protein in high-density lipoprotein (HDL), and other lipoproteins are found in the corona around many nanoparticles, but data on protein structural and functional effects are lacking. Here we investigate the structural consequences of the adsorption of apoAI, apolipoprotein B100 (apoB100), and HDL on polystyrene nanoparticles with different surface charges.

Tensin2 reduces intracellular phosphatidylinositol 3,4,5-trisphosphate levels at the plasma membrane.

Tensins are proposed cytoskeleton-regulating proteins. However, Tensin2 additionally inhibits Akt signalling and cell survival. Structural modelling of the Tensin2 phosphatase (PTPase) domain revealed an active site-like pocket receptive towards phosphoinositides.

Modeling the time evolution of the nanoparticle-protein corona in a body fluid.

Background: Nanoparticles in contact with biological fluids interact with proteins and other biomolecules, thus forming a dynamic corona whose composition varies over time due to continuous protein association and dissociation events. Eventually equilibrium is reached, at which point the continued exchange will not affect the composition of the corona.

Results: We developed a simple and effective dynamic model of the nanoparticle protein corona in a body fluid, namely human plasma.