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Influence of protein configuration on aggregation kinetics of nanoplastics in aquatic environment

Water Research 2022 69 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count. Score: 55 ? 0–100 AI score estimating relevance to the microplastics field. Papers below 30 are filtered from public browse.
Dehua Zeng, Dehua Zeng, Dehua Zeng, Ziqing Huang, Sijia Liu, Yanjun Liu, Ziqing Huang, Dehua Zeng, Ziqing Huang, Chen Yang, Weilin Huang Weilin Huang Chengyu Chen, Chengyu Chen, Chengyu Chen, Ziqing Huang, Ziqing Huang, Ziqing Huang, Ziqing Huang, Ziqing Huang, Chen Yang, Dehua Zeng, Weilin Huang Chengyu Chen, Dehua Zeng, Weilin Huang Yanjun Liu, Chen Yang, Ziqing Huang, Ziqing Huang, Chen Yang, Ziqing Huang, Ziqing Huang, Chen Yang, Chengyu Chen, Sijia Liu, Weilin Huang Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Chen Yang, Dehua Zeng, Ziqing Huang, Ziqing Huang, Sijia Liu, Dehua Zeng, Ziqing Huang, Ziqing Huang, Zhi Dang, Zhi Dang, Chengyu Chen, Chen Yang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Chen Yang, Zhi Dang, Zhi Dang, Weilin Huang Weilin Huang Weilin Huang Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Zhi Dang, Weilin Huang Zhi Dang, Zhi Dang, Weilin Huang Weilin Huang Chen Yang, Weilin Huang Weilin Huang Weilin Huang Chen Yang, Weilin Huang Chengyu Chen, Chengyu Chen, Weilin Huang Zhi Dang, Chengyu Chen, Chen Yang, Chengyu Chen, Zhi Dang, Weilin Huang Zhi Dang, Weilin Huang Weilin Huang Chengyu Chen, Weilin Huang Chen Yang, Zhi Dang, Chengyu Chen, Chengyu Chen, Chengyu Chen, Weilin Huang Chengyu Chen, Zhi Dang, Chengyu Chen, Chengyu Chen, Chen Yang, Zhi Dang, Weilin Huang

Summary

Researchers investigated how five different proteins with varying structures affect the aggregation behavior of polystyrene nanoplastics in water under different ionic strength and pH conditions. They found that protein type and configuration significantly influenced whether nanoplastics clumped together or remained dispersed, with globular proteins like albumin having different effects than fibrous proteins like collagen. The study suggests that the protein composition of natural waters plays an important role in determining how nanoplastics behave and transport in aquatic environments.

Polymers
Body Systems

Aggregation kinetics of nanoplastics in aquatic environment are influenced by their interactions with proteins having different structures and properties. This study employed time-resolved dynamic light scattering (TR-DLS) to investigate the effects of 5 proteins (bovine hemoglobin (BHb), bovine (BSA) and human serum albumin (HSA), collagen type I (Col I), and bovine casein (CS)) on aggregation kinetics of polystyrene nanoplastics (PSNPs) under natural water conditions, which were simulated using various ionic strength (1-1000 mM NaCl and 0.01-100 mM CaCl), pH (3-9), and protein concentration (1-5 mg/L of total organic carbon). The results indicated that the interactions between proteins and PSNPs strongly depended on electrostatic properties, protein structures, and solution chemistries, which induced distinct aggregation behaviors in NaCl and CaCl solutions. Electrostatic repulsion and steric hindrance dominated their interactions in NaCl solution by stabilizing PSNPs with the order of spherical BSA and disordered CS > heart-shaped HSA > fibrillar Col I; whereas positively charged BHb destabilized PSNPs with aggregation rate of 1.71 nm/s at 300 mM NaCl. In contrast, at CaCl concentration below 20 mM, proteins destabilized PSNPs following the sequence of HSA > BHb > Col I > BSA depending on counterbalance among double layer compression, cation bridging, and steric hindrance; whereas CS stabilized PSNPs by precipitating Ca that inhibited charge screening effect. Both protein concentration and solution pH affected protein corona formation, surface charge, and protein structure that altered stability of PSNPs. Characterizations using fluorescence spectroscopy, circular dichroism, and two-dimensional correlation analysis spectroscopy showed fluorescence quenching and ellipticity reduction of proteins, indicating strong adsorption affinity between PSNPs and proteins. The study provides insight to how protein configuration and water chemistry affect fate and transport of nanoplastics in aquatic environment.

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