Multi-spectroscopic measurements, molecular modeling and density functional theory calculations for interactions of 2,7-dibromocarbazole and 3,6-dibromocarbazole with serum albumin.

2,7-Dibromocarbazole (2,7-DBCB) and 3,6-dibromocarbazole (3,6-DBCB) are emerging environmental pollutants, being potentially high risks to human health. In this study, interactions of the two compounds with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated by molecular modeling, density functional theory calculations (DFT) and multispectral techniques. The static quenching interaction deduced in the fluorescence quenching experiment is confirmed by the time-resolved analyses. The interactions of the two compounds with HSA/BSA induce molecular microenvironment and conformation changes, as assessed by synchronous and 3D fluorescence spectra, together with a destruction of polypeptide carbonyl hydrogen bond network by circular dichroism and Fourier transform infrared analyses. The thermodynamic analysis indicated that the spontaneous interaction was hydrogen bonding and hydrophobic forces. The binding constant Ka at 298 K was 3.54 × 105 M−1 in HSA-2,7-DBCB, 6.63 × 105 M−1 in HSA-3,6-DBCB, 1.32 × 105 M−1 in BSA-2,7-DBCB and 2.17 × 105 M−1 in BSA-3,6-DBCB. These results indicates that 3,6-DBCB binds HSA/BSA more strongly than 2,7-DBCB, which was estimated with DFT calculations. Site marker competition experiments coupled with molecular modeling studies confirmed that both compounds bind HSA/BSA at site I (subdomain IIA). The results suggest that interactions between 2,7-DBCB and 3,6-DBCB with HSA and BSA may affect the normal physiological activities in human and animals. Unlabelled Image • 3,6-DBCB binds HSA and BSA stronger than 2,7-DBCB. • 2,7-DBCB and 3,6-DBCB bind HSA and BSA at site I (subdomain IIA). • The bindings changed the microenvironment and conformation. [ABSTRACT FROM AUTHOR]