Interaction between Halogenated Phenols and Thyroxine‐Binding Protein: A Multispectral and Computational Approach

• DOI: 10.1002/slct.202401288
• Publication Date: 2024-08-14T10:20:46Z
• Authors: Wenhui Liang; Yanting Chen; Muwei Huang; Zeyu Song; Cancan Li; Yanhong Zheng; Zhongsheng Yi
• Keywords: Docking (animal)

Abstract The aim of this study was to understand the interaction between transthyretin (TTR) and halogenated phenols (HPs) including 2,4‐dichlorophenol (DCP), 2,4,6‐trichlorophenol (TCP), pentachlorophenol (PCP), 2‐bromophenol (2‐BP), 2,4‐dibromophenol (DBP) 2,4,6‐tribromophenol (TBP). Computer simulation multi‐spectroscopy techniques were used investigate interaction. fluorescence TTR found be quenched through static quenching non‐radiative energy transfer by HPs, suggesting that binding process HPs primarily influenced van der Waals forces hydrogen bonds. ANS substitution experiments indicated interacted with at T4 site. Three‐dimensional spectra Fourier transform infrared spectroscopy conformational microenvironmental changes resulting from interactions HPs. Additionally, molecular docking reduced density gradient analysis identify specific residues involved in sites. findings subsequently validated quantum chemical analysis. This research integrates state‐of‐the‐art multispectral analytical methodologies sophisticated computational modeling introduce an innovative approach for dissecting (TTR). methodology offers a novel avenue investigating interplay TTR, thereby providing critical insights are instrumental assessing latent toxicity these compounds.