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.