Volume 41, Issue 2, December 2023, Pages 390–412
Andry Hariniaina RABEARISOA1, Hajandrainy RABEARISOA2, and Xinghui Xia3
1 Sciences et technologies, Ecole Normale Supérieur, Fianarantsoa, Madagascar
2 Sciences et technologies, Ecole Normale Supérieur, Fianarantsoa, Madagascar
3 School of Environment, Beijing Normal University, State Key Laboratory of Water Environment Simulation, Key Laboratory for Water and Sediment Sciences (Ministry of Education), Beijing 100875, China
Original language: English
Copyright © 2023 ISSR Journals. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
This research in this aspect is necessary, because of PFASs are one kind of hydrophobic and hydrophilic chemicals, and the study of PFASs with protein used as a dissolved organic matter in this study is valuable to evaluate the ecological risk of this kind of chemicals. Fluorescence has been proven as a sensible method to provide qualitative and quantitative information on the PFAS-serum albumin interactions. This work will provide some information for appropriately understanding the interaction between PFASs and protein and illustrate its binding mechanisms at different concentration of protein, cations and pH. The results obtained from fluorescence spectra indicated that PFASs could quench the intrinsic fluorescence of protein through a static quenching procedure, with the effective quenching constants (K’sv) varying from 0.44 105 L mol-1 to 5.73 105 L mol-1. It infers that the complex of PFAS-protein was formed. In addition, the ionic strength and pH affected the effective quenching constant of PFASs bound to bovine albumin. Furthermore, with increase of pH from 6.5 to 8.5, reduction in the binding affinity of PFAS to bovine albumin and soy peptone were also observed. The interaction between perfluoroalkyl substances and protein using fluorescence spectroscopy, and the occurrence of electrostatic interactions with hydrophobic force in the binding also studied.
Author Keywords: Perfluoroalkyl substances (PFASs), Bioaccumulation, Protein, Dissolved organic matter (DOM), Cations, Fluorescence quenching.
Andry Hariniaina RABEARISOA1, Hajandrainy RABEARISOA2, and Xinghui Xia3
1 Sciences et technologies, Ecole Normale Supérieur, Fianarantsoa, Madagascar
2 Sciences et technologies, Ecole Normale Supérieur, Fianarantsoa, Madagascar
3 School of Environment, Beijing Normal University, State Key Laboratory of Water Environment Simulation, Key Laboratory for Water and Sediment Sciences (Ministry of Education), Beijing 100875, China
Original language: English
Copyright © 2023 ISSR Journals. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
This research in this aspect is necessary, because of PFASs are one kind of hydrophobic and hydrophilic chemicals, and the study of PFASs with protein used as a dissolved organic matter in this study is valuable to evaluate the ecological risk of this kind of chemicals. Fluorescence has been proven as a sensible method to provide qualitative and quantitative information on the PFAS-serum albumin interactions. This work will provide some information for appropriately understanding the interaction between PFASs and protein and illustrate its binding mechanisms at different concentration of protein, cations and pH. The results obtained from fluorescence spectra indicated that PFASs could quench the intrinsic fluorescence of protein through a static quenching procedure, with the effective quenching constants (K’sv) varying from 0.44 105 L mol-1 to 5.73 105 L mol-1. It infers that the complex of PFAS-protein was formed. In addition, the ionic strength and pH affected the effective quenching constant of PFASs bound to bovine albumin. Furthermore, with increase of pH from 6.5 to 8.5, reduction in the binding affinity of PFAS to bovine albumin and soy peptone were also observed. The interaction between perfluoroalkyl substances and protein using fluorescence spectroscopy, and the occurrence of electrostatic interactions with hydrophobic force in the binding also studied.
Author Keywords: Perfluoroalkyl substances (PFASs), Bioaccumulation, Protein, Dissolved organic matter (DOM), Cations, Fluorescence quenching.
How to Cite this Article
Andry Hariniaina RABEARISOA, Hajandrainy RABEARISOA, and Xinghui Xia, “Interaction between PFASs and protein using Fluorescence spectroscopy,” International Journal of Innovation and Applied Studies, vol. 41, no. 2, pp. 390–412, December 2023.
