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

•Noncovalent interactions of 24 diverse OH-PBDEs with BSA are examined by ESI-MS.•BSA preferentially interacts with one OH-octaBDE and two OH-heptaBDE isomers.•OH-PBDEs are inferred to be bound as both neutral and anionic species.•Possible conformational changes in BSA induced on binding are explored by IM-MS.

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

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