  Nanoparticle (NP)-protein complexes exhibit the correct identity of NP in
biological media. Therefore, protein-NP interactions should be closely explored
to understand and to modulate the nature of NPs in medical implementations.
This review focuses mainly on the physicochemical parameters such as dimension,
surface chemistry, the morphology of NPs and influence of medium pH on the
formation of protein corona and conformational changes of adsorbed proteins by
different kinds of methods. Also, the impact of protein corona on the colloidal
stability of NPs is discussed. Uncontrolled protein attachment on NPs may bring
unwanted impacts such as protein denaturation and aggregation. In contrast,
controlled protein adsorption by optimal concentration, size, pH and surface
modification of NPs may result in potential implementation of NPs as
therapeutic agents especially for disaggregation of amyloid fibrils. Also, the
effect of NPs-protein corona on reducing the cytotoxicity and clinical
implications such as drug delivery, cancer therapy, imaging and diagnosis will
be discussed. Validated correlative physicochemical parameters for NP-protein
corona formation frequently derived from protein corona fingerprints of NPs
which are more valid than the parameters obtained only on the base of NP
features. This review may provide useful information regarding the potency as
well as the adverse effects of NPs to predict their behavior in the in vivo
experiments.
