Table 2.
Nanomaterials | Incubation Medium | Protein Corona Compositions | Inference | Ref. |
---|---|---|---|---|
Iron oxideNPs/SPION | FBS | Anti-thrombin, α-antiproteinase, and serotransferrin. | Polyvinyl alcohol (PVA)-coated SPIONs with (−) and (+) surface charge had a higher adsorption rate in serum proteins than the dextran-coated SPIONs that led to a higher circulation time in blood in the case of PVA-coated NPs compared to the dextran-coated SPIONs. | [21] |
Magnetic NPs | Human blood serum and human lymph serum | Serum albumin, Apolipoprotein A-I, Prothrombin, Plasminogen, Complement protein, Apolipoprotein B-100, Apolipoprotein E, Antithrombin-III, Vitronectin, and Kininogen-1 | Hard protein corona (HPCs) received by two isolation methods were entirely different by upto 50%, which suggested that only these proteins that were found in the HPCs fromboth magnetic separation and multistep centrifugation methods were real HPCs. | [22] |
Artificial viral NPs with AuNPs | Blood serum | Reported presence of hard and soft corona on nanoparticles. Despite corona evolution over NPs, GM3 enclosed in the AVN membrane remained approachable to CD169 receptor binding. | The bigger particles with low DOPS % showed a higher stability in serum plasma. As a result, a increased layering of PC led to a lowering in the targeting of GM3 for CD169. Further, study is required to give insight into the formation of PC with regard to AVN in vitro, although this extends key points of relevance to PC layering on NP size and fate in the biological environment | [29] |
AuNPs | - | Serum albumin, Alpha-2-Macroglobulin, Apolipoprotein A-I, Apolipoprotein E, Complement factor H, Plasminogen, Ig mu chain C region, Protein Ighv7–1. | The results indicated from the gel electrophoresis and mass spectrometry analysis that the development of the complex with protein coronas, took place within 10 min of injection. | [30] |
Gold nanostructures (spheres, rods, stars, and cages) | 70% human serum (diluted with PBS) for 2 h | The 15 most abundant proteins were associated AuNPs. Some of them were Serum albumin, Apolipoprotein E, Coagulation factor XII, Apolipoprotein A-I and A-II, Kininogen-1, Gelsolin, Vitronectin, Histidine-rich glycoprotein. | The cage-like structure of AuNPs indicated the lowest adsorbed corona proteins. The results revealed that nano-cages could improve the compatibility with the biological medium compared with other shapes due to the high area of curvature and the heavy ligation over flat surfaces that opposes opsonization and the rapid clearance via the immune system. | [32] |
Nanoparticles (silica, polystyrene, and carboxyl-modified polystyrene particles) | Human plasma; plasma with cytosolic fluid | Tubulin alpha-1, Alpha-enolase, Nucleophosmin, Protein S100-A9, 60S ribosomal protein L14, PEST proteolytic signal-containing nuclear protein, Triosephosphate isomerase, Protein S100-A9. | The results have shown that abundant protein corona could evolve in the IInd biological solution, but the last protein left a “fingerprint” of its history. This is important to map the evolution and understand how the pathway was generated for adsorption to the nanoparticles, and eventually to predict the fate and behavior of the nanoparticles. | [35] |
PSCOOH, PSOSO3H, and silica particles (SiO2) | Blood plasma | Hard and soft corona particles on the nanoparticle surface altered their surface chemistry. | Formation of hard or soft corona protein assembly and their longevity depends upon the nanomaterial type. The blood plasma-derived protein coronas have a long life. Rather than appearing over the surface of the nanomaterial, this is actually what the cell sees. | [19] |
CS NPs | FBS, biological buffer, and serum | Protein coronas of different compositions | Protein corona adsorption on the HA-chitosan nanoparticle influenced the interaction with the HA-receptor i.e., CDD4 mediated cellular uptake. | [37] |
Colloidal silica nanoparticles |
FBS in Phosphate Buffer Saline (PBS) | Protein corona of varying molecular weight ranges (MW< 17 kDa to >135 kDa) were accessed on the silica particle according to the protein band intensity. | The colloidal destability of the nanoparticles was overcome by adding depletant polymers, Pluronic-F127 and PEG, of different molecular weights. The interaction between the polymer and the nanoparticle had a minimal impact on protein access by the nanoparticle surface upon incubation with serum. The serum protein had a significant effect on the corona profile compared to other polymers. | [9] |
AgNPs | Model protein environments for the self-evolution of corona | Model protein BSA | These polymers, polyethyleneimine (PEI), polyvinylpyrrolidone (PVP), and poly(2-vinyl pyridine)-b-poly(ethylene oxide) (PEO-b-P2VP) were applied as stabilizing agents. The PEO-b-P2VP and PVP-stabilized nanoparticles were reported to be inert to the protein’s adsorption. The PEI-stabilized AgNPs had substantial interactions with BSA. | [10] |