Influences of protein-corona on stability and aggregation kinetics of Ti 3 C 2 T x nanosheets in aquatic environment

Proteins existed in aquatic environments strongly influence the transport, fate of nanomaterials due to the formation of protein-corona surrounding nanomaterials. To date, how do proteins affect the aggregation behaviors of MXene, a new family of two-dimensional materials, in aquatic environment rem...

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Bibliographic Details
Published in:Environmental research 2023-02, Vol.219, p.115131
Main Authors: Cheng, Shizhu, Tan, Feng, Wu, Xuri, Dong, Fan, Liu, Jinghua, Wang, Yan, Zhao, Hongxia
Format: Article
Language:English
Subjects:
Kinetics
Nanostructures
Protein Corona
Titanium
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Summary:Proteins existed in aquatic environments strongly influence the transport, fate of nanomaterials due to the formation of protein-corona surrounding nanomaterials. To date, how do proteins affect the aggregation behaviors of MXene, a new family of two-dimensional materials, in aquatic environment remains unknown. Here the aggregation kinetics of MXene Ti C T nanosheets in various electrolytes (NaCl, CaCl and Na SO ) was investigated by time-resolved dynamic light scattering in absence or presence of bovine serum albumin (BSA). Results showed that BSA affected the aggregation of Ti C T in a concentration-dependent manner. Addition of 3 mg/L BSA decreased the critical coagulation concentrations (CCCs) of Ti C T about 1.6-2.1 times, showing obvious destabilization effect; while BSA greater than 30 mg/L created a high-protein environment covering Ti C T , producing high spatial repulsion and enhancing the dispersibility of Ti C T . Ca ions have greater effect on the aggregation of Ti C T due to the larger surface charge and bridging effect. The interaction between Ti C T and BSA followed Derjaguin-Landau-Verwey-Overbeek (DLVO) theory, and mainly attributed to hydrogen bonding and van der Waals forces, while positively charged lysine and arginine in BSA might attract onto Ti C T through electrostatic attraction. The interaction decreased the content of α-helix structure in BSA from 74.7% to 53.1%. Ti C T easily suffered from aggregation and their long-distance transport seemed impossible in synthetic or natural waters. The present findings provided new insights for understanding the transfer and fate of this nanomaterial in aquatic environments.
ISSN:1096-0953
DOI:10.1016/j.envres.2022.115131