Biomedical Engineering Reference
In-Depth Information
Fig. 2.1
Schematic illustration of soft and hard protein corona and the concept of the rate of
adsorption and desorption which determines the exchange time and lifetime of proteins in the
protein corona. The hard or soft corona is not composed of only a single protein; in this scheme, the
complexity of the presence of different proteins is not shown
subset of the plasma adsorbome binds to most nanomaterials, and only a fraction of
the adsorbome is bound to a nanomaterial with high abundance.
The competitive adsorption of proteins on the limited surface of nanoparticles
containing the collective effects of incubation time, concentration of protein, and
adsorption affinity between protein and nanoparticle surface is called “Vroman
effect” [
4
,
5
].
2.1.1 Hard Corona
A review of literature shows that varying nanoparticles with various surface
modifications have been studied by different methods to find out the composition
of their protein corona. A summary of these studies is provided by Aggarwal et al.
[
5
] which shows that albumin, immunoglobulin G (IgG), fibrinogen, and
apolipoproteins are present in the corona of all the studied nanoparticles. These
proteins have high abundance in blood plasma, and therefore, at later times, they
might be replaced by proteins with lower concentration but higher affinity to the
nanoparticle surface. Lundqvist et al. [
6
] have studied “hard” corona formed around
nanoparticles of different materials, including copolymer and polystyrene
nanoparticles, of different sizes, and with different surface properties.
One of the mechanisms of adsorption of proteins on the surface of nanoparticles
is the entropy-driven binding. The mechanism of entropy-driven-bonded proteins
such as fibrinogen, lysozyme, ovalbumin, and human carbonic anhydrase II is the
release of bound water from the surface of the nanoparticle. In this case,
the increase in entropy of released water molecules is larger than the decrease in
