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.

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
1秒前
zp560应助mxy126354采纳,获得200
1秒前
ccxr发布了新的文献求助10
5秒前
Indexxx发布了新的文献求助10
5秒前
YHL发布了新的文献求助10
5秒前
5秒前
6秒前
虚拟的棉花糖完成签到,获得积分10
6秒前
8秒前
zyy发布了新的文献求助10
9秒前
壮观道罡完成签到,获得积分10
10秒前
11秒前
呼呼螺发布了新的文献求助30
11秒前
科研渊发布了新的文献求助10
12秒前
斯文败类应助YHL采纳,获得10
13秒前
落寞的鸡发布了新的文献求助10
15秒前
15秒前
15秒前
思源应助Evan采纳,获得10
17秒前
丁久洋发布了新的文献求助10
19秒前
ini发布了新的文献求助10
19秒前
20秒前
xiaofan_www发布了新的文献求助10
20秒前
Dylan完成签到,获得积分10
21秒前
21秒前
虫虫太可爱了吧完成签到,获得积分10
22秒前
ephore应助yu采纳,获得30
23秒前
上官若男应助狗十七采纳,获得10
23秒前
寂寞的诗云完成签到,获得积分10
24秒前
24秒前
亮亮完成签到,获得积分10
24秒前
蓝天发布了新的文献求助10
25秒前
ZJM完成签到,获得积分10
27秒前
28秒前
28秒前
赘婿应助xiaofan_www采纳,获得10
28秒前
呼呼螺完成签到 ,获得积分20
29秒前
张炜钰完成签到,获得积分10
30秒前
30秒前
Lw完成签到,获得积分10
31秒前
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
PowerCascade: A Synthetic Dataset for Cascading Failure Analysis in Power Systems 2000
Various Faces of Animal Metaphor in English and Polish 800
Signals, Systems, and Signal Processing 610
Photodetectors: From Ultraviolet to Infrared 500
On the Dragon Seas, a sailor's adventures in the far east 500
Yangtze Reminiscences. Some Notes And Recollections Of Service With The China Navigation Company Ltd., 1925-1939 500
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 物理 内科学 复合材料 催化作用 物理化学 光电子学 电极 细胞生物学 基因 无机化学
热门帖子
关注 科研通微信公众号,转发送积分 6354092
求助须知:如何正确求助?哪些是违规求助? 8169101
关于积分的说明 17196078
捐赠科研通 5410215
什么是DOI,文献DOI怎么找? 2863906
邀请新用户注册赠送积分活动 1841349
关于科研通互助平台的介绍 1689961