Biomedical Engineering Reference
In-Depth Information
Table 2.4
The role of nanoparticle's physicochemical and environmental parameters on the
protein corona
The parameter The observed effect
Higher charge density of NP - Increases density and thickness of corona
- Charge particle has higher opsonization rate
- Increases protein conformal change
Higher hydrophobicity of NP - Increases the thickness of protein corona
- Increases protein conformal change
- Hydrophobicity increases the opsonization rate
Higher curvature of NP - Increases the corona thickness
- Decreases the conformational change
- Does not change the identity of adsorbed proteins
Higher protein concentration in environment - Higher thickness
- Change in the identity of adsorbed proteins
Some of the data is adapted from the tabulated data in [
2
,
5
]
plasma protein onto the surface of two commercially available nanoparticles
(hydrophobic carboxylated polystyrene (PSOSO
3
) and hydrophilic silica (SiO
2
)
NPs) were probed. The results showed that apolipoproteins leaved the composition
of protein corona following nanoparticle passing low-concentrated proteins to the
high-concentrated protein environments (see Figs.
2.10
and
2.11
).
2.6 Conclusion
Upon entrance of nanomaterials inside biological environment, proteins start to
adsorb on the surface in a competitive manner. The formation of protein layer on
the surface is called protein corona which is composed of a hard and a soft region
with strong and weak binding to the surface, respectively. Various parameters can
affect the composition, thickness, and conformation of these layers which are
summarized in Table
2.4
. In addition, there are several ignored factored including
temperature, protein source pathways, and cell vision, which should be considered
in future.
References
1. Monopoli MP, Walczyk D, Campbell A, Elia G, Lynch I, Bombelli FB, Dawson KA (2011)
Physical-chemical aspects of protein corona: relevance to in vitro and in vivo biological
impacts of nanoparticles. J Am Chem Soc 133:2525-2534
2. Walkey CD, Chan WC (2012) Understanding and controlling the interaction of nanomaterials
with proteins in a physiological environment. Chem Soc Rev 41:2780-2799
3. Simberg D, Park JH, Karmali PP, Zhang WM, Merkulov S, McCrae K, Bhatia SN, Sailor M,
Ruoslahti E (2009) Differential proteomics analysis of the surface heterogeneity of dextran
