PDBsum entry 6xv0

Transport protein

PDB id: 6xv0

Contents

Protein chain

581 a.a.

Ligands

MYR ×6

M6O ×2

PDB id:

6xv0

Name:

Transport protein

Title:

Lauric acid functionalized hexamolybdoaluminate bound to human serum albumin

Structure:

Serum albumin. Chain: a

Source:

Homo sapiens. Human. Organism_taxid: 9606

Resolution:

3.00Å R-factor: 0.269 R-free: 0.311

Authors:

A.Bijelic,A.Dobrov,A.Roller,A.Rompel

Key ref:

A.Bijelic et al. (2020). Binding of a Fatty Acid-Functionalized Anderson-Type Polyoxometalate to Human Serum Albumin. Inorg Chem, 59, 5243-5246. PubMed id: 32255347 DOI: 10.1021/acs.inorgchem.9b03407

Date:

21-Jan-20 Release date: 18-Mar-20

Protein chain

P02768  (ALBU_HUMAN) -  Albumin from Homo sapiens

Seq: 609 a.a.

Struc: 581 a.a.

DOI no: 10.1021/acs.inorgchem.9b03407

Inorg Chem 59:5243-5246 (2020)

PubMed id: 32255347

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

A.Bijelic, A.Dobrov, A.Roller, A.Rompel.

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.