Investigation of noncovalent interactions between hydroxylated polybrominated diphenyl ethers and bovine serum albumin using electrospray ionization-ion mobility-mass spectrometry

摘要: Abstract The noncovalent interactions of 24 diversely structured hydroxylated polybrominated diphenyl ethers (OH-PBDEs), ranging from monobromodiphenyl ether (OH-monoBDE) to octabromodiphenyl (OH-octaBDE), with bovine serum albumin (BSA) have been examined by employing an electrospray ionization source fitted on a quadrupole time-of-flight hybrid mass spectrometer equipped traveling wave ion mobility cell. spectrometric parameters were finely optimized favor the observation complexes. experimental data confirm that due close structural resemblance thyroid hormone thyroxine, some OH-PBDEs shown conjugate BSA. It is found BSA preferentially interacts one OH-octaBDE (4′-OH-BDE-201) and two heptabromodiphenyl (OH-heptaBDE) isomers (4-OH-BDE-187 6-OH-BDE-180) 1:1 2:1 binding stoichiometries. state bound inferred be as both neutral anionic species. dissociation constants corresponding complexes are calculated titration curve fitting. Investigation into various OH-PBDE analogs demonstrates degree bromination positions hydroxylation bromine moieties may exert influence possible conformational changes in induced upon explored use mobility-mass spectrometry (IM-MS) understand details aspects.