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Nanoparticle-protein interaction is one of the important aspects of xenobiotic materials in biological
environments. Larger nanoparticles can effect on proteins structure and caused more decrements in
their hydrophilicity. All proteins have certain binding affinity to nanoparticles called, Vroman effect.
This effect is coupled with free Gibbs energy alteration in energy profile of free proteins and their
adsorbed on nanoparticles. However, there are no evidences that show how and why hard corona is
a protein fingerprint. This study showed that, larger proteins having higher molecular weight and
less helix structures attitude to larger nanoparticles. According to statistical analysis, unlike
previous studies, it found that the size of nanoparticles is more important than their hydrophobicity.
From a thermodynamic point of view, larger nanoparticles have more contact positions than the
smaller; so whole energy transmitted from larger nanoparticles is higher. This result indicated that
the energy transmitted from smaller nanoparticles to protein, could be transferred to aqueous
environment more than larger ones. In addition it demonstrated that, energy parameter could be
used as reference parameter for explaining protein attitude to nanoparticle. Whereas nanoparticles
can play a role as seeds for protein fibrillation, it is important to consider that how they selected for
a specific experiment. For example, in targeted drug delivery systems, nanoparticles act as good
carriers. So according to nanoparticles characteristics and protein features in target cells, tissues
and organisms nanoparticle-protein interactions could be predicted and then experimentally tested
with respect to decrements in probability errors.
Keywords: Thermodynamic interaction, Corona, Free Gibbs energy, Protein fibrillation