AI Article Synopsis
- The study explored how various Zr-substituted polyoxometalates (Zr-POMs) affect the hydrolysis of transferrin, a blood plasma glycoprotein, at pH 7.4.
- The incubation of transferrin with Zr-POMs led to the formation of 13 polypeptide fragments, with hydrolysis efficiency varying by the type of Zr-POM used.
- Investigative techniques like tryptophan fluorescence, circular dichroism, and phosphorus NMR spectroscopy were employed to understand molecular interactions and how they influence the reactivity and structural changes of transferrin.
Article Abstract
The hydrolysis of the iron-binding blood plasma glycoprotein transferrin (Tf) has been examined at pH = 7.4 in the presence of a series of Zr-substituted polyoxometalates (Zr-POMs) including Keggin (EtNH)[Zr(PWO)]∙7HO (), (EtNH)[{-PWOZr-(-OH) (HO)}]∙7HO (), Wells-Dawson KH[Zr(-PWO)]·25HO (), Na[Zr(-PWO)(-O)(-OH)(HO)]·57HO () and Lindqvist (MeN)[ZrWO(HO)] (), (nBuN)[(ZrWO(-OH))]∙2HO ()) type POMs. Incubation of transferrin with Zr-POMs resulted in formation of 13 polypeptide fragments that were observed on sodium dodecyl sulfate poly(acrylamide) gel electrophoresis (SDS-PAGE), but the hydrolysis efficiency varied depending on the nature of Zr-POMs. Molecular interactions between Zr-POMs and transferrin were investigated by using a range of complementary techniques such as tryptophan fluorescence, circular dichroism (CD), P-NMR spectroscopy, in order to gain better understanding of different efficiency of investigated Zr-POMs. A tryptophan fluorescence quenching study revealed that the most reactive species show the strongest interaction toward transferrin. The CD results demonstrated that interaction of Zr-POMs and transferrin in buffer solution result in significant secondary structure changes. The speciation of Zr-POMs has been followed by P-NMR spectroscopy in the presence and absence of transferrin, providing insight into stability of the catalysts under reaction condition.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7435656 | PMC |
| http://dx.doi.org/10.3390/molecules25153472 | DOI Listing |
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Article Synopsis
- The study explored how various Zr-substituted polyoxometalates (Zr-POMs) affect the hydrolysis of transferrin, a blood plasma glycoprotein, at pH 7.4.
- The incubation of transferrin with Zr-POMs led to the formation of 13 polypeptide fragments, with hydrolysis efficiency varying by the type of Zr-POM used.
- Investigative techniques like tryptophan fluorescence, circular dichroism, and phosphorus NMR spectroscopy were employed to understand molecular interactions and how they influence the reactivity and structural changes of transferrin.
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