6533b834fe1ef96bd129e272

RESEARCH PRODUCT

Effect of Core-Crosslinking on Protein Corona Formation on Polymeric Micelles.

Christian LepsStefan TenzerIrina AlbergStefan KramerRudolf Zentel

subject

Polymers and PlasticsChemical PhenomenaLightPolymersNanoparticleBioengineeringProtein Corona02 engineering and technology010402 general chemistry01 natural sciencesMicelleMass SpectrometryPolyethylene GlycolsBiomaterialsCorona (optical phenomenon)PlasmaDynamic light scatteringMaterials ChemistryCopolymerHumansScattering RadiationChromatography High Pressure LiquidMicellesGel electrophoresisChemistry021001 nanoscience & nanotechnologyBlood proteins0104 chemical sciencesNanostructuresCross-Linking ReagentsBiophysicsProtein CoronaAdsorption0210 nano-technologyHydrophobic and Hydrophilic InteractionsBiotechnology

description

Most nanomaterials acquire a protein corona upon contact with biological fluids. The magnitude of this effect is strongly dependent both on surface and structure of the nanoparticle. To define the contribution of the internal nanoparticle structure, protein corona formation of block copolymer micelles with poly(N-2-hydroxypropylmethacrylamide) (pHPMA) as hydrophilic shell, which are crosslinked-or not-in the hydrophobic core is comparatively analyzed. Both types of micelles are incubated with human blood plasma and separated by asymmetrical flow field-flow fractionation (AF4). Their size is determined by dynamic light scattering and proteins within the micellar fraction are characterized by gel electrophoresis and quantified by liquid chromatography-high-resolution mass spectrometry-based label-free quantitative proteomics. The analyses reveal only very low amounts of plasma proteins associated with the micelles. Notably, no significant enrichment of plasma proteins is detectable for core-crosslinked micelles, while noncrosslinked micelles show a significant enrichment of plasma proteins, indicative of protein corona formation. The results indicate that preventing the reorganization of micelles (equilibrium with unimers) by core-crosslinking is crucial to reduce the interaction with plasma proteins.

10.1002/mabi.202000414https://pubmed.ncbi.nlm.nih.gov/33543588