4.8 Article

Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Journal

ACS APPLIED MATERIALS & INTERFACES
Volume -, Issue -, Pages -

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acsami.2c11874

Keywords

protein corona; quantum dots; chirality; fluorescence resonance energy transfer; protein adsorption

Funding

  1. National Youth Talents Programme, Project of Intergovernmental International Science and Technology Innovation Cooperation [2022YFE0113000]
  2. State Key Laboratory of Solidification Processing (NPU) , China [2020-QZ-01]

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This study established a FRET-based platform for monitoring the dynamic evolution of protein corona in complex biological media. The nature of initially adsorbed proteins on quantum dots significantly affects subsequent exchange behavior, with only a limited proportion of proteins being involved in the exchange process, which is also significantly influenced by the surface chirality of the quantum dots.
Elucidating the biological behavior of engineered nanoparticles, for example, the protein corona, is important for the development of safe and efficient nanomedicine, but our current understanding is still limited due to its highly dynamic nature and lack of adequate analytical tools. In the present work, we demonstrate the establishment of a fluorescence resonance energy transfer (FRET)-based platform for monitoring the dynamic evolution behavior of the protein corona in complex biological media. With human serum albumin and lysozyme as the model serum proteins, the protein exchange process of the preformed corona on the surface of chiral quantum dots (QDs) upon feeding either individual protein or human serum was monitored in situ by FRET. Important parameters characterizing the evolution process of protein corona could be obtained upon quantitative analysis of FRET data. Further combining real-time FRET monitoring with gel electrophoresis experiments revealed that the nature of the protein initially adsorbed on the surface of QDs significantly affects the subsequent dynamic exchange behavior of the protein corona. Furthermore, our results also revealed that only a limited proportion of proteins are involved in the protein exchange, and the exchange process exhibits a significant dependence on the surface chirality of QDs. This work demonstrates the feasibility of FRET as a powerful tool to exploit the dynamic evolution process of the protein corona, which can provide theoretical guidance for further design of advanced nanomaterials for biomedical applications.

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