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

化学 圆二色性 动态光散射 牛血清白蛋白 动力学 离子强度 疏水效应 荧光 结晶学 水动力半径 位阻效应 生物物理学 分析化学(期刊) 化学工程 色谱法 立体化学 水溶液 有机化学 物理 工程类 生物 纳米颗粒 量子力学 胶束
作者
Ziqing Huang,Chengyu Chen,Yanjun Liu,Sijia Liu,Dehua Zeng,Chen Yang,Weilin Huang,Zhi Dang
出处
期刊:Water Research [Elsevier BV]
卷期号:219: 118522-118522 被引量:42
标识
DOI:10.1016/j.watres.2022.118522
摘要

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 CaCl2), 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 CaCl2 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 CaCl2 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 Ca2+ 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.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
cij123完成签到,获得积分10
7秒前
爱是无限大完成签到,获得积分0
11秒前
科研通AI6.3应助zxxx采纳,获得10
12秒前
勤qin完成签到 ,获得积分10
13秒前
蓝色花生豆完成签到,获得积分0
16秒前
19秒前
无尘完成签到 ,获得积分10
23秒前
zxxx发布了新的文献求助10
24秒前
99完成签到 ,获得积分10
28秒前
呆萌冰彤完成签到 ,获得积分10
30秒前
我要读博士完成签到 ,获得积分10
30秒前
田様应助科研通管家采纳,获得10
43秒前
思源应助科研通管家采纳,获得10
43秒前
隐形曼青应助科研通管家采纳,获得10
43秒前
43秒前
桐桐应助科研通管家采纳,获得30
43秒前
小蘑菇应助科研通管家采纳,获得20
43秒前
43秒前
44秒前
orixero应助科研通管家采纳,获得10
44秒前
JamesPei应助科研通管家采纳,获得20
44秒前
99完成签到 ,获得积分10
55秒前
科研通AI6.1应助英吉利25采纳,获得10
58秒前
369ninja发布了新的文献求助10
1分钟前
1分钟前
1分钟前
1分钟前
俗人完成签到 ,获得积分10
1分钟前
独孤刘完成签到,获得积分10
1分钟前
1分钟前
飒卡完成签到 ,获得积分10
1分钟前
希望天下0贩的0应助369ninja采纳,获得10
1分钟前
1分钟前
nicky完成签到 ,获得积分10
1分钟前
1分钟前
和平港湾完成签到,获得积分10
1分钟前
悦耳的怀寒应助和平港湾采纳,获得10
1分钟前
连国完成签到 ,获得积分10
1分钟前
kanong完成签到,获得积分0
1分钟前
共享精神应助wj采纳,获得10
1分钟前
高分求助中
(应助此贴封号)【重要!!请各用户(尤其是新用户)详细阅读】【科研通的精品贴汇总】 10000
Cronologia da história de Macau 5000
Petrology and Plate Tectonics 800
Electrode Potentials 550
Matrix Methods in Data Mining and Pattern Recognition 510
Trees of tropical Asia : an illustrated guide to diversity 500
Materials Informatics Molecules, Crystals and Beyond A volume in Acta Materialia Book Series 400
热门求助领域 (近24小时)
化学 材料科学 医学 生物 纳米技术 工程类 有机化学 化学工程 生物化学 计算机科学 内科学 物理 复合材料 催化作用 细胞生物学 无机化学 光电子学 物理化学 电极 基因
热门帖子
关注 科研通微信公众号,转发送积分 7042936
求助须知:如何正确求助?哪些是违规求助? 8709687
关于积分的说明 18444619
捐赠科研通 6554425
什么是DOI,文献DOI怎么找? 3117351
关于科研通互助平台的介绍 2201542
邀请新用户注册赠送积分活动 2092749