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The interactions of methylphenanthrene (MP) isomers (1-MP, 3-MP, 4-MP, and 9-MP) with human serum albumin (HSA) were studied in simulated physiological conditions. A fluorescence analysis revealed that each MP formed a 1:1 ground-state complex with HSA. The binding constants at 308 K decreased in the order of 3-MP (9.13 × 10 4  L·mol −1 ) &gt; 9-MP (3.57 × 10 4  L·mol −1 ) &gt; 4-MP (2.37 × 10 4  L·mol −1 ) &gt; 1-MP (1.46 × 10 4  L·mol −1 ), which was consistent with the docking results. The  Kb  values at 298 K, 308 K, and 318 K revealed that the  β -isomer has a stronger binding affinity with HSA than the  α -isomer. Thermodynamic and docking parameters showed that MPs combined with HSA through van der Waals forces. The results of the binding site competition experiment and molecular docking indicated that 4-MP bound at subdomain IIA in HSA molecule, while the other MPs bound at a site between subdomains IB and IIA. The circular dichroism (CD) spectra showed that the  α -helical content of HSA reduced in the presence of 1-MP, 4-MP and 9-MP, while no significant change was observed in the presence of 3-MP. Further, the fluorescence spectroscopic studies revealed that the Vitamin B 2  (VB 2 )-transporting function of HSA was inhibited by 3-MP and 9-MP, and enhanced by 1-MP and 4-MP. Moreover, the impact degrees of MPs on the VB 2 -transporting function had a positive correlation with the binding affinities of the MPs to HSA.HighlightsInteractions of MP isomers methylated at varying sites with HSA were studied.The  α -substituted MP had a weaker affinity to HSA than  β -substituted MP.Binding site of 4-MP in HSA was different from that of 1-MP/3-MP/9-MP.MP isomers unfolded the  α -helical structure of HSA to varying degrees.Transporting function of HSA was inhibited by 3-MP/9-MP but enhanced by 1-MP/4-MP. Interactions of MP isomers methylated at varying sites with HSA were studied. The  α -substituted MP had a weaker affinity to HSA than  β -substituted MP. Binding site of 4-MP in HSA was different from that of 1-MP/3-MP/9-MP. MP isomers unfolded the  α -helical structure of HSA to varying degrees. Transporting function of HSA was inhibited by 3-MP/9-MP but enhanced by 1-MP/4-MP.

polycyclic aromatic compounds

Study on the Binding of Methylphenanthrene Isomers with Different Methylated Positions to Human Serum Albumin Employing Spectroscopic Techniques Combined with Molecular Docking