The interactions between human serum albumin (HSA) and α1- acid glycoprotein (AGP), the main plasma proteins binding drugs/xenobiotics, and some endocrine disrupting chemicals (EDCs), such as bisphenol A (BPA) and some of its structural analogues, bisphenol S (BPS), bisphenol F (BPF), bisphenol E (BPE), bisphenol B (BPB), bisphenol AF (BPAF), bisphenol A diglycidyl ether (BADGE) and bisphenol M (BPM), were characterized by biomimetic liquid chromatography (LC). The interactions between bisphenols (BPs) and either HSA or AGP protein was found to be non-specific and essentially lipophilicity-driven. To get more information on the binding of BPs and plasma proteins, in silico predictions and molecular docking simulations were exploited, and the results achieved in silico were compared to those observed in vitro. BPM was the one exhibiting the highest affinity on both plasma proteins according to these data. Our findings clarified the binding of these EDCs to plasma proteins and offered insights into the biodistribution and bioaccumulation processes underlying their toxicity.