Binding of a Fatty Acid-Functionalized Anderson-Type Polyoxometalate to Human Serum Albumin

Abstract

The Anderson-type hexamolybdoaluminate functionalized with lauric acid (LA), (TBA)₃[Al(OH)₃Mo₆O₁₈{(OCH₂)₃CNHCOC₁₁H₂₃}]·9H₂O (TBA-AlMo₆-LA, where TBA = tetrabutylammonium), was prepared via two synthetic routes and characterized by thermogravimetric and elemental analyses, mass spectrometry, IR and ¹H NMR spectroscopy, and powder and single-crystal X-ray diffraction. The interaction of TBA-AlMo₆-LA with human serum albumin (HSA) was investigated via fluorescence and circular dichroism spectroscopy. The results revealed that TBA-AlMo₆-LA binds strongly to HSA (63% quenching at an HSA/TBA-AlMo₆-LA ratio of 1:1), exhibiting static quenching. In contrast to TBA-AlMo₆-LA, the nonfunctionalized polyoxometalate, Na₃(H₂O)₆[Al(OH)₆Mo₆O₁₈]·2H₂O (AlMo₆), showed weak binding toward HSA (22% quenching at a HSA/AlMo₆ ratio of 1:25). HSA binding was confirmed by X-ray structure analysis of the HSA-Myr-AlMo₆-LA complex (Myr = myristate). These results provide a promising lead for the design of novel polyoxometalate-based hybrids that are able to exploit HSA as a delivery vehicle to improve their pharmacokinetics and bioactivity.