Plasma protein corona forming upon fullerene nanocomplex: Impact on both counterparts--颗粒学报PARTICUOLOGY

Wu, L., Fu, F., Wang, W., Wang, W., Huang, Z., Huang, Y., . . . Wu, C. (2023). Plasma protein corona forming upon fullerene nanocomplex: Impact on both counterparts. Particuology, 73, 26-36. https://doi.org/10.1016/j.partic.2022.04.006

Plasma protein corona forming upon fullerene nanocomplex: Impact on both counterparts

Linjing Wu ^a, Fangqin Fu ^a, Wenhao Wang ^b, Wenhua Wang ^b, Zhengwei Huang ^a *, Ying Huang ^a, Xin Pan ^b, Chuanbin Wu ^a

a College of Pharmacy, Jinan University, Guangzhou, 510632, China
b School of Pharmaceutical Sciences, Sun Yat-Sen University, Guangzhou, 510006, China

10.1016/j.partic.2022.04.006

Volume 73, February 2023, Pages 26-36

Received 26 September 2021, Revised 21 March 2022, Accepted 12 April 2022, Available online 4 May 2022, Version of Record 16 May 2022.

E-mail: huangzhengw@jnu.edu.cn

Highlights

• Interaction between C60 nanocomplex and plasma proteins was investigated.

• Related binding mechanisms of C60 nanocomplex and proteins were explored.

• C60 nanocomplex induced fibrinogen to aggregate, which might cause side effects.

• C60 nanocomplex could induce conformational changes of different proteins.

Abstract

Protein corona refers to the structure composed of biomolecules adsorbed on the surface of nanomaterials. The study on the effect of the interaction between protein and nanoparticles can provide an important guide for the application of nanodrug delivery. To provide a reference for the research on fullerene (C60) nanocomplex drug delivery systems, this work studied the interaction between C60 nanocomplex and a variety of plasma proteins. Research showed that the protein binding with C60 nanocomplex did not change the charge properties of protein. The proteins induced the aggregation of C60 nanocomplex. The circular dichroism spectra showed that the secondary structure of the proteins changed after binding to C60 nanocomplex. The ultraviolet–visible spectra showed that the effect of C60 nanocomplex on proteins was concentration-dependent. The fluorescence spectra showed that C60 nanocomplex could intrinsic fluorescence alteration of proteins. The adsorption capacity of C60 nanocomplex to proteins was changed at 0 h and 4 h. The interaction between nanocomplex and proteins might affect the morphological characteristics of nanocomplex and the conformation of proteins. This work could provide a reference for the research and development of C60 nanocomplex and other carbon-based nanocomplex as nanoparticulate drug delivery systems.

Graphical abstract

Keywords

Fullerene; Nanocomplex; Interaction; Protein corona

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