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Protein corona, understanding the nanoparticle-protein interactions and future perspectives: A critical review

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ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.12.108

关键词

Protein corona; Protein-nanoparticle interactions; Protein adsorption

资金

  1. Zonguldak Bulent Ecevit University [2016-72118496-08]

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Proteins are diverse biopolymers that participate in almost all processes in living cells. When nanoparticles interact with proteins, they form a protein corona layer, which influences their interactions. The characteristics of nanoparticles such as size, surface chemistry, and charge play a critical role in determining the behavior of the protein corona.
Proteins are biopolymers of highly varied structures taking part in almost all processes occurring in living cells. When nanoparticles (NPs) interact with proteins in biological environments, they are surrounded by a layer of biomolecules, mainly proteins adsorbing to the surfaces. This protein rich layer formed around NPs is called the protein corona. Consequential interactions between NPs and proteins are governed due to the characteristics of the corona. The features of NPs such as the size, surface chemistry, charge are the critical factors influencing the behavior of protein corona. Molecular properties and protein corona composition affect the cellular uptake of NPs. Understanding and analyzing protein corona formation in relation to protein-NP properties, and elucidating its biological implications play an important role in bio-related nano-research studies. Protein-NP interactions have been studied extensively for the purpose of investigating the potential use of NPs as carriers in drug delivery systems. Further study should focus on exploring the effects of various characteristic parameters, such as the particle size, modifier type, temperature, pH on protein-NP interactions, providing toxicity information of novel NPs. In this contribution, important aspects related to protein corona forming, influential factors, novel findings and future perspectives on protein-NP interactions are overviewed. (C) 2020 Elsevier B.V. All rights reserved.

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