Evaluation of the binding of perfluorinated compound to pepsin: Spectroscopic analysis and molecular docking. (October 2016)

• Record Type: Journal Article
• Authors: Yue, Yuanyuan; Sun, Yangyang; Yan, Xuyang; Liu, Jianming; Zhao, Shufang; Zhang, Jia
• Is Part Of: Chemosphere. Volume 161(2016)
• Page Start: 475
• Page End: 481
• Publication Date: 2016-10
• Subjects: Perfluorinated compound -- Digestive enzymes -- Binding mechanism -- Fluorescence; Pollution -- Periodicals; Pollution -- Physiological effect -- Periodicals; Environmental sciences -- Periodicals; Atmospheric chemistry -- Periodicals; 551.511
• DOI: 10.1016/j.chemosphere.2016.07.047
• Languages: English
• ISSNs: 0045-6535

Abstract

Abstract: In this paper, we investigated the binding mode of perfluorooctanoic acid (PFOA) and perfluorononanoic acid (PFNA) to pepsin using spectroscopies and molecular docking methods. Fluorescence quenching study indicated that their different ability to bind with pepsin. Meanwhile, time-resolved fluorescence measurements established that PFOA and PFNA quenched the fluorescence intensity of pepsin through the mechanism of static quenching. The thermodynamic parameters showed that hydrophobic forces were the main interactions. Furthermore, UV-vis, FTIR, three-dimensional fluorescence and molecular docking result indicated that PFCs impact the conformation of pepsin and PFOA was more toxic than PFNA. The conformational transformation of PFOA/PFNA-pepsin was confirmed through the quantitative analysis of the CD spectra. The present studies offer the theory evidence to analyze environmental safety and biosecurity of PFCs on proteases. Highlights: The interaction mechanism between pepsin and perfluorinated chemicals (PFOA, PFNA) was investigated in vitro. The binding affinity of PFOA/PFNA with pepsin was explored detailed. The conformation of pepsin has been changed after PFOA/PFNA binding.