Unknown

Dataset Information

0

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.

SUBMITTER: Bijelic A 

PROVIDER: S-EPMC7175456 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Bijelic Aleksandar A   Dobrov Anatolie A   Roller Alexander A   Rompel Annette A  

Inorganic chemistry 20200407 8


The Anderson-type hexamolybdoaluminate functionalized with lauric acid (LA), (TBA)<sub>3</sub>[Al(OH)<sub>3</sub>Mo<sub>6</sub>O<sub>18</sub>{(OCH<sub>2</sub>)<sub>3</sub>CNHCOC<sub>11</sub>H<sub>23</sub>}]·9H<sub>2</sub>O (TBA-AlMo<sub>6</sub>-LA, where TBA = tetrabutylammonium), was prepared via two synthetic routes and characterized by thermogravimetric and elemental analyses, mass spectrometry, IR and <sup>1</sup>H NMR spectroscopy, and powder and single-crystal X-ray diffraction. The intera  ...[more]

Similar Datasets

| S-EPMC6532450 | biostudies-literature
| S-EPMC2596408 | biostudies-literature
| S-EPMC4504500 | biostudies-literature
| S-EPMC2134860 | biostudies-literature
| S-EPMC5740134 | biostudies-literature
| S-EPMC9309503 | biostudies-literature
| S-EPMC7980502 | biostudies-literature
| S-EPMC6554544 | biostudies-literature
| S-EPMC7737218 | biostudies-literature
| S-EPMC166163 | biostudies-literature