Characterization of the interaction between triclosan and catalase

• Published in: RSC advances Vol. 7; no. 15; pp. 931 - 936
• Main Authors: Zou, Luyi, Mi, Chenyu, Yu, Hongyan, Gu, Wenxiu, Teng, Yue
• Format: Journal Article
• Language: English
• Published: Cambridge Royal Society of Chemistry 01.01.2017
• Subjects: Antiinfectives and antibacterials; Antioxidants; Assessments; Binding sites; Catalase; Docking; Ecological monitoring; Holes; Molecular docking; Pollutants; Product safety; Safety; Toxicity
• ISSN: 2046-2069; 2046-2069
• DOI: 10.1039/c6ra26431j

Triclosan (TCS), as a kind of broad spectrum antimicrobial agent, is widely used in personal care products. However, its effectiveness and safety are met with much skepticism. High exposure of TCS to the environment poses a potential threat to ecological safety and human health. In this article, we investigated the interaction between TCS and the antioxidant enzyme catalase (CAT) using spectroscopic techniques and molecular docking technologies. The experimental results showed that TCS could bind into the central cavity of CAT with one binding site to form a TCS-CAT complex, and the main force was the hydrophobic effect. The interaction made some changes to the conformation and micro-environment of CAT and inhibited the activity of CAT. This work explored the interaction between TCS and CAT at the molecular level, which could help us to understand the toxicity mechanism of TCS and provide a reference for pollutant toxicity assessments. The interaction between triclosan (TCS) and the antioxidant enzyme catalase (CAT) was investigated and could help us to understand the toxicity mechanism of TCS and provide a reference for pollutant toxicity assessments.