Molecular modeling study reveals subclass-specific binding mechanisms of flame retardants to human serum albumin, highlighting distinct chemical drivers of pollutant transport.
Key Points
Investigate the molecular binding mechanisms and physicochemical drivers governing interactions between various brominated flame retardants and human serum albumin.
Performed molecular docking to predict binding affinities, binding modes, and key interacting amino acid residues for diverse brominated flame retardant subclasses.
Conducted 100 ns molecular dynamics simulations to evaluate complex stability and performed correlation analyses between chemical properties and binding affinities.
Docking revealed binding energies from −6.32 to −10.98 kcal·mol⁻¹, with stabilization driven by hydrophobic interactions, hydrogen bonds, and halogen bonds involving residues PHE104A, LEU70A, and ILE73A.
Molecular dynamics trajectories demonstrated stable binding poses, with protein backbone root-mean-square deviation (RMSD) values remaining between 0.20 and 0.45 nm across 100 ns.
Binding determinants were subclass-specific: affinity correlated significantly with molecular weight for PBBs (r = 0.646, p ≤ 0.05) and with density for PBDEs (r = 0.5045, p ≤ 0.05).