Novel amphoteric starch-stabilized nanoparticles exhibit excellent protein corona-free properties and also functionalized by antibodies to achieve excellent targeting and cell internalization capabilities for their use in photodynamic therapy.
The protein corona on nanoparticles
(NPs) is a critical problem
that often screens the targeting molecules and becomes one of the
key reasons for the lack of practical application in nanotherapy.
It is critical to fully understand the mechanism of the nanoparticle–biological
interactions to design the nanoparticle-based therapeutic agents.
Some types of proteins can be precoated on the nanoparticles to avoid
unwanted protein attachment; however, the ultralow level of protein
corona is hard to achieve, and the relationship of the antifouling
property of the precoated protein nanoparticles with protein conformation
and protein–nanoparticle interaction energy has never been
investigated. In this work, we provided the quantitative protein corona
composition analysis on different precoated protein nanoparticles,
and on the basis of the molecular simulation process, we found their
antifouling property strongly depended on the interaction energy of
the precoated protein–serum protein pair and the number of
hydrogen bonds formed between them. Furthermore, it also depended
on the nanoparticle–serum protein pair interaction energy and
the protein conformation on the nanoparticle. The casein coated nanoparticle
with the antifouling property was determined, and after aptamer conjugation
and drug loading, they exhibited superior targeting and internalization
behavior for photodynamic and photothermal therapy in vitro and in
vivo. Our work adds to the understanding of the protein corona behavior
of precoated protein nanoparticles, and the determined antifouling
NP can potentially be used as a highly efficient nanodrug carrier.
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