Biomedical Engineering Reference
In-Depth Information
Table 2.1
Identification of proteins bound to nanoparticles by gel electrophoresis and mass
spectrometry [
24
]
Nanoparticles Proteins
TiO
2
Albumin, fibrinogen (
chains), histidine-rich glycoprotein, kininogen-1,
complement C9 and C1q, Ig heavy chain (
α
and
β
γ
), fetuin A, vitronectin, apolipo-
protein A1
SiO
2
Albumin, fibrinogen (
α
,
β
and
γ
chains), complement C8, Ig heavy chain (gamma,
kappa), apolipoprotein A
ZnO
Albumin, Ig heavy chain (alpha, mu, gamma), apolipoprotein A1, immunoglobulin
(J chain), alpha-2-macroglobulin, transferrin, alpha-1-antichymotryspin
group and coatings on the protein corona is not fully developed yet and more studies
are still required to let us tailor the composition of the protein corona with surface
treatment of nanoparticles.
Surface functionalization with PEG of varying chain length resulted in major
changes in organ/tissue-selective biodistribution and clearance from the body,
although 2D gel electrophoresis showed that immune-competent proteins (IgG,
fibrinogen) bind much more than albumins irrespective of PEG chain length.
Numerous studies established that aqueous suspensions of nonfunctionalized
nanoparticles are stabilized against agglomeration by the addition of bovine/human
serum albumin (BSA/HSA) and some other proteins. The effect has also been
exploited in production for the debundling and dispersion of graphene and CNT
material. Especially albumins in water or Dulbecco's Modified Eagle Medium
(DMEM) have dispersed and stabilized a wide variety of nanomaterials: CNTs,
metal nanoparticles, metal carbide nanoparticles, and metal oxide nanoparticles.
2.4.4 Hydrophilicity/Hydrophobicity
The hydrophobicity affects both the amount of adsorbed protein as well as the
composition of protein corona. The enhanced adsorption of proteins on hydropho-
bic surface in comparison with hydrophilic surface increases the rate of
opsonization of hydrophobic nanoparticles [
5
].
Hydrophobic or charged surfaces tend to adsorb more proteins and denature
them with a greater extent than neutral and hydrophilic surfaces. For example,
increasing the negative charge density and hydrophobicity of polystyrene
nanoparticles increases protein adsorption from plasma, and more hydrophobic
copolymer
nanoparticles
adsorb more
protein
than
their
hydrophilic
counterparts [
15
].
Hydrophobic nanoparticles adsorb more albumin molecules than hydrophilic
nanoparticles, even though the affinity of the protein to both nanoparticle types is
roughly the same [
25
]. This suggests that hydrophobic copolymer nanoparticles
have more protein-binding sites. This may result from “clustering” of
the
