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

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ID: 106773
2020
The Anderson-type hexamolybdoaluminate functionalized with lauric acid (LA), (TBA)[Al(OH)MoO{(OCH)CNHCOCH}]·9HO (TBA-AlMo-LA, where TBA = tetrabutylammonium), was prepared via two synthetic routes and characterized by thermogravimetric and elemental analyses, mass spectrometry, IR and H NMR spectroscopy, and powder and single-crystal X-ray diffraction. The interaction of TBA-AlMo-LA with human serum albumin (HSA) was investigated via fluorescence and circular dichroism spectroscopy. The results revealed that TBA-AlMo-LA binds strongly to HSA (63% quenching at an HSA/TBA-AlMo-LA ratio of 1:1), exhibiting static quenching. In contrast to TBA-AlMo-LA, the nonfunctionalized polyoxometalate, Na(HO)[Al(OH)MoO]·2HO (AlMo), showed weak binding toward HSA (22% quenching at a HSA/AlMo ratio of 1:25). HSA binding was confirmed by X-ray structure analysis of the HSA-Myr-AlMo-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.
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Authors Bijelic, Aleksandar;Dobrov, Anatolie;Roller, Alexander;Rompel, Annette;
Journal Inorganic chemistry
Year 2020
DOI 10.1021/acs.inorgchem.9b03407
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