6XV0

lauric acid functionalized hexamolybdoaluminate bound to human serum albumin

Summary for 6XV0

• Entry DOI: 10.2210/pdb6xv0/pdb
• Descriptor: Serum albumin, MYRISTIC ACID, lauric acid functionalized hexamolybdoaluminate (3 entities in total)
• Functional Keywords: serum protein, complex, polyoxometalate, transport protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 70419.49

Authors

Bijelic, A.,Dobrov, A.,Roller, A.,Rompel, A. (deposition date: 2020-01-21, release date: 2020-03-18, Last modification date: 2024-01-24)

Primary citation

Bijelic, A.,Dobrov, A.,Roller, A.,Rompel, A.
Binding of a Fatty Acid-Functionalized Anderson-Type Polyoxometalate to Human Serum Albumin.
Inorg.Chem., 59:5243-5246, 2020

PubMed Abstract: 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.

PubMed: 32255347
DOI: 10.1021/acs.inorgchem.9b03407

Experimental method

X-RAY DIFFRACTION (3 Å)