Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin
The potential health risks posed by the coexistence of nanoplastics (NPs) and triclosan (TCS) have garnered significant attention. However, the effects and underlying mechanisms of NPs and TCS on key functional proteins at the molecular level remain poorly understood. This study reports the effect o...
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2025-01-01
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| author | Yan Bao Yaoyao Wang Hongbin Liu Jing Lan Zhicai Li Wansong Zong Zongshan Zhao |
| author_facet | Yan Bao Yaoyao Wang Hongbin Liu Jing Lan Zhicai Li Wansong Zong Zongshan Zhao |
| author_sort | Yan Bao |
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| description | The potential health risks posed by the coexistence of nanoplastics (NPs) and triclosan (TCS) have garnered significant attention. However, the effects and underlying mechanisms of NPs and TCS on key functional proteins at the molecular level remain poorly understood. This study reports the effect of polystyrene nanoplastics (PSNPs) on the binding of TCS to human serum albumin (HSA) using multispectral methods and molecular simulation systems. The experimental results show that TCS significantly inhibits HSA esterase activity, with exacerbating inhibition in the presence of PSNPs, which is attributed to the alteration of HSA conformation and microenvironment of the amino acid residues induced by PSNPs. Molecular docking and site marker competitive studies indicate that TCS predominantly binds to site I of subdomain Sudlow II and the presence of PSNPs does not affect the binding sites. Spectra analyses indicate that the quenching mechanism between TCS and HSA belongs to the static quenching type and the presence of PSNPs does not change the fluorescence quenching type. The HSA fluorescence quenching and the conformational alterations induced by TCS are further enhanced in the presence of PSNPs, indicating that PSNPs enhance the binding of TCS to HSA by making TCS more accessible to the binding sites. This study provides valuable information about the toxicity of PSNPs and TCS in case of co-exposure. |
| format | Article |
| id | doaj-art-b1e171d025574a5dadfef5ba1a0b2382 |
| institution | Kabale University |
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| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
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| series | Life |
| spelling | doaj-art-b1e171d025574a5dadfef5ba1a0b23822025-01-24T13:38:50ZengMDPI AGLife2075-17292025-01-0115111210.3390/life15010112Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum AlbuminYan Bao0Yaoyao Wang1Hongbin Liu2Jing Lan3Zhicai Li4Wansong Zong5Zongshan Zhao6Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, Qingdao 266237, ChinaSchool of Environment and Geography, Qingdao University, Qingdao 266071, ChinaSchool of Environment and Geography, Qingdao University, Qingdao 266071, ChinaSchool of Environment and Geography, Qingdao University, Qingdao 266071, ChinaAnqiu Branch of Weifang Municipal Bureau of Ecology and Environment, Weifang 262199, ChinaCollege of Geography and Environment, Shandong Normal University, Jinan 250014, ChinaSchool of Environment and Geography, Qingdao University, Qingdao 266071, ChinaThe potential health risks posed by the coexistence of nanoplastics (NPs) and triclosan (TCS) have garnered significant attention. However, the effects and underlying mechanisms of NPs and TCS on key functional proteins at the molecular level remain poorly understood. This study reports the effect of polystyrene nanoplastics (PSNPs) on the binding of TCS to human serum albumin (HSA) using multispectral methods and molecular simulation systems. The experimental results show that TCS significantly inhibits HSA esterase activity, with exacerbating inhibition in the presence of PSNPs, which is attributed to the alteration of HSA conformation and microenvironment of the amino acid residues induced by PSNPs. Molecular docking and site marker competitive studies indicate that TCS predominantly binds to site I of subdomain Sudlow II and the presence of PSNPs does not affect the binding sites. Spectra analyses indicate that the quenching mechanism between TCS and HSA belongs to the static quenching type and the presence of PSNPs does not change the fluorescence quenching type. The HSA fluorescence quenching and the conformational alterations induced by TCS are further enhanced in the presence of PSNPs, indicating that PSNPs enhance the binding of TCS to HSA by making TCS more accessible to the binding sites. This study provides valuable information about the toxicity of PSNPs and TCS in case of co-exposure.https://www.mdpi.com/2075-1729/15/1/112human serum albumininteraction mechanismnanoplasticstriclosan |
| spellingShingle | Yan Bao Yaoyao Wang Hongbin Liu Jing Lan Zhicai Li Wansong Zong Zongshan Zhao Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin Life human serum albumin interaction mechanism nanoplastics triclosan |
| title | Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin |
| title_full | Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin |
| title_fullStr | Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin |
| title_full_unstemmed | Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin |
| title_short | Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin |
| title_sort | co existing nanoplastics further exacerbates the effects of triclosan on the physiological functions of human serum albumin |
| topic | human serum albumin interaction mechanism nanoplastics triclosan |
| url | https://www.mdpi.com/2075-1729/15/1/112 |
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