Comprehensive insights into the interactions of dicyclohexyl phthalate and its metabolite to human serum albumin

Phthalate esters (PAEs) are a type of persistent organic pollutants and have received widespread concerns due to their adverse effects on human health. Dicyclohexyl phthalate (DCHP) and its metabolite monocyclohexyl phthalate (MCHP) were selected to explore the mechanism for interaction of PAEs with human serum albumin (HSA) through molecular docking and several spectroscopic techniques. The results showed that DCHP/MCHP can spontaneously occupy site I to form a binary complex with HSA, and DCHP exhibited higher binding affinity to HSA than MCHP. At 298 K, the binding constants (Kb) of DCHP and MCHP to HSA were 24.82 x 10(4) and 1.04 x 10(4) M-1, respectively. Hydrogen bonds and van der Waals forces were the major driving forces in DCHP/ MCHP-HSA complex. The presence of DCHP/MCHP induced the secondary structure changes in HSA, and the pi electrons of the benzene ring skeleton of DCHP/MCHP played a key role in this binding processes. Exposure of DCHP/MCHP to TM4 cells revealed that interactions between PAEs and serum albumin can affect their cytotoxicity; DCHP showed higher toxicity than MCHP. The binding affinity of PAEs with HSA may be a valuable parameter for rapid assessment of their toxicity to organisms.

Automated summary

Phthalate esters are persistent organic pollutants that have adverse effects on human health. Through molecular docking and spectroscopic techniques, it was found that DCHP has higher binding affinity to HSA compared to MCHP, leading to changes in the protein's secondary structure and increased cytotoxicity. Understanding the binding affinity of PAEs with HSA may provide valuable insights for assessing their toxicity to organisms.