Understanding the Regioselective Hydrolysis of Human Serum Albumin by Zr(IV)-Substituted Polyoxotungstates Using Tryptophan Fluorescence Spectroscopy

Inorganics

Vincent Goovaerts²  Karen Stroobants²  Gregory Absillis²  Tatjana N. Parac-Vogt¹  Greta Ricarda Patzke² 

[1] Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Heverlee, Belgium;

关键词: polyoxometalates;    tryptophan fluorescence;    artificial metalloproteases;   

DOI  :  10.3390/inorganics3020230

来源: mdpi

【 摘 要 】

The interaction between human serum albumin (HSA) and a series of Zr(IV)-substituted polyoxometalates (POMs) (Lindqvist type POM ((ⁿBu₄N)₆[{W₅O₁₈Zr(μ-OH)}₂]·2H₂O, Zr2-L2), two Keggin type POMs ((Et₂NH₂)₁₀[Zr(PW₁₁O₃₉)₂]·7H₂O, Zr1-K2 and (Et₂NH₂)₈[{α-PW₁₁O₃₉Zr(μ-OH)(H₂O)}₂]·7H₂O, Zr2-K2), and two Wells-Dawson type POMs (K₁₅H[Zr(α₂-P₂W₁₇O₆₁)₂]·25H₂O, Zr1-WD2 and Na₁₄[Zr₄(P₂W₁₆O₅₉)₂(μ₃-O)₂(OH)₂(H₂O)₄]·10H₂O, Zr4-WD2) was investigated by tryptophan (Trp) fluorescence spectroscopy. The fluorescence data were analyzed using the Tachiya model, ideally suited for multiple binding site analysis. The obtained quenching constants have the same order of magnitude for all the measured POM:protein complexes, ranging from 1.9 × 10⁵ M⁻¹ to 5.1 × 10⁵ M⁻¹. The number of bound POM molecules to HSA was in the range of 1.5 up to 3.5. The influence of the ionic strength was studied for the Zr1-WD2:HSA complex in the presence of NaClO₄. The calculated quenching constant decreases upon increasing the ionic strength of the solution from 0.0004 M to 0.5004 M, indicating the electrostatic nature of the interaction. The number of POM molecules bound to HSA increases from 1.0 to 4.8. ³¹P NMR spectroscopy provided evidence for the stability of all investigated POM structures during the interaction with HSA.

【 授权许可】

CC BY   
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