posted on 2024-03-12, 20:13authored byZhenduo Zhang, Xuepeng Dong, Wang Wan, Hengke Guo, Rui Sun, Huan Feng, Mengdie Wang, Zhiming Wang, Hao Jin, Jialu Sun, Qiuxuan Xia, Qi Zhao, Di Shen, Zhenming Gao, Yu Liu
Bioaccumulation of nanoplastic particles has drawn increasing
attention
regarding environmental sustainability and biosafety. How nanoplastic
particles interact with the cellular milieu still remains elusive.
Herein, we exemplify a general approach to profile the composition
of a “protein corona” interacting with nanoparticles
via the photocatalytic protein proximity labeling method. To enable
photocatalytic proximity labeling of the proteome interacting with
particles, iodine-substituted BODIPY (I-BODIPY) is selected as the
photosensitizer and covalently conjugated onto amino-polystyrene nanoparticles
as a model system. Next, selective proximity labeling of interacting
proteins is demonstrated using I-BODIPY-labeled nanoplastic particles
in both Escherichia coli lysate and
live alpha mouse liver 12 cells. Mechanistic studies reveal that the
covalent modifications of proteins by an aminoalkyne substrate are
conducted via a reactive oxygen species photosensitization pathway.
Further proteomic analysis uncovers that mitochondria-related proteins
are intensively involved in the protein corona, indicating substantial
interactions between nanoplastic particles and mitochondria. In addition,
proteostasis network components are also identified, accompanied by
consequent cellular proteome aggregation confirmed by fluorescence
imaging. Together, this work exemplifies a general strategy to interrogate
the composition of the protein corona of nanomaterials by endowing
them with photooxidation properties to enable photocatalytic protein
proximity labeling function.