Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates
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 (Et<sub>2</sub>NH<sub>2</sub>)<sub>10</sub>[Zr(PW<sub>11<...
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| Format: | Article |
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MDPI AG
2020-07-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/15/3472 |
| _version_ | 1827712023219142656 |
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| author | Laura S. Van Rompuy Nada D. Savić Alvaro Rodriguez Tatjana N. Parac-Vogt |
| author_facet | Laura S. Van Rompuy Nada D. Savić Alvaro Rodriguez Tatjana N. Parac-Vogt |
| author_sort | Laura S. Van Rompuy |
| collection | DOAJ |
| description | 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 (Et<sub>2</sub>NH<sub>2</sub>)<sub>10</sub>[Zr(PW<sub>11</sub>O<sub>39</sub>)<sub>2</sub>]∙7H<sub>2</sub>O (<b>Zr-K 1:2</b>), (Et<sub>2</sub>NH<sub>2</sub>)<sub>8</sub>[{<i>α</i>-PW<sub>11</sub>O<sub>39</sub>Zr-(<i>μ</i>-OH) (H<sub>2</sub>O)}<sub>2</sub>]∙7H<sub>2</sub>O (<b>Zr-K 2:2</b>), Wells-Dawson K<sub>15</sub>H[Zr(<i>α</i><sub>2</sub>-P<sub>2</sub>W<sub>17</sub>O<sub>61</sub>)<sub>2</sub>]·25H<sub>2</sub>O (<b>Zr-WD 1:2</b>), Na<sub>14</sub>[Zr<sub>4</sub>(<i>α</i>-P<sub>2</sub>W<sub>16</sub>O<sub>59</sub>)<sub>2</sub>(<i>μ</i><sub>3</sub>-O)<sub>2</sub>(<i>μ</i>-OH)<sub>2</sub>(H<sub>2</sub>O)<sub>4</sub>]·57H<sub>2</sub>O (<b>Zr-WD 4:2</b>) and Lindqvist (Me<sub>4</sub>N)<sub>2</sub>[ZrW<sub>5</sub>O<sub>18</sub>(H<sub>2</sub>O)<sub>3</sub>] (<b>Zr-L 1:1</b>), (nBu<sub>4</sub>N)<sub>6</sub>[(ZrW<sub>5</sub>O<sub>18</sub>(<i>μ</i>–OH))<sub>2</sub>]∙2H<sub>2</sub>O (<b>Zr-L 2:2</b>)) 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), <sup>31</sup>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 <b>Zr-WD</b> 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 <sup>31</sup>P-NMR spectroscopy in the presence and absence of transferrin, providing insight into stability of the catalysts under reaction condition. |
| first_indexed | 2024-03-10T18:05:31Z |
| format | Article |
| id | doaj.art-b8eefff941134e0cb435e84b790bb35d |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T18:05:31Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-b8eefff941134e0cb435e84b790bb35d2023-11-20T08:31:36ZengMDPI AGMolecules1420-30492020-07-012515347210.3390/molecules25153472Selective Hydrolysis of Transferrin Promoted by Zr-Substituted PolyoxometalatesLaura S. Van Rompuy0Nada D. Savić1Alvaro Rodriguez2Tatjana N. Parac-Vogt3Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven, BelgiumDepartment of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven, BelgiumDepartment of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven, BelgiumDepartment of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven, BelgiumThe 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 (Et<sub>2</sub>NH<sub>2</sub>)<sub>10</sub>[Zr(PW<sub>11</sub>O<sub>39</sub>)<sub>2</sub>]∙7H<sub>2</sub>O (<b>Zr-K 1:2</b>), (Et<sub>2</sub>NH<sub>2</sub>)<sub>8</sub>[{<i>α</i>-PW<sub>11</sub>O<sub>39</sub>Zr-(<i>μ</i>-OH) (H<sub>2</sub>O)}<sub>2</sub>]∙7H<sub>2</sub>O (<b>Zr-K 2:2</b>), Wells-Dawson K<sub>15</sub>H[Zr(<i>α</i><sub>2</sub>-P<sub>2</sub>W<sub>17</sub>O<sub>61</sub>)<sub>2</sub>]·25H<sub>2</sub>O (<b>Zr-WD 1:2</b>), Na<sub>14</sub>[Zr<sub>4</sub>(<i>α</i>-P<sub>2</sub>W<sub>16</sub>O<sub>59</sub>)<sub>2</sub>(<i>μ</i><sub>3</sub>-O)<sub>2</sub>(<i>μ</i>-OH)<sub>2</sub>(H<sub>2</sub>O)<sub>4</sub>]·57H<sub>2</sub>O (<b>Zr-WD 4:2</b>) and Lindqvist (Me<sub>4</sub>N)<sub>2</sub>[ZrW<sub>5</sub>O<sub>18</sub>(H<sub>2</sub>O)<sub>3</sub>] (<b>Zr-L 1:1</b>), (nBu<sub>4</sub>N)<sub>6</sub>[(ZrW<sub>5</sub>O<sub>18</sub>(<i>μ</i>–OH))<sub>2</sub>]∙2H<sub>2</sub>O (<b>Zr-L 2:2</b>)) 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), <sup>31</sup>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 <b>Zr-WD</b> 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 <sup>31</sup>P-NMR spectroscopy in the presence and absence of transferrin, providing insight into stability of the catalysts under reaction condition.https://www.mdpi.com/1420-3049/25/15/3472polyoxometalatezirconiummetalloproteasestransferrinhydrolysis |
| spellingShingle | Laura S. Van Rompuy Nada D. Savić Alvaro Rodriguez Tatjana N. Parac-Vogt Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates Molecules polyoxometalate zirconium metalloproteases transferrin hydrolysis |
| title | Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates |
| title_full | Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates |
| title_fullStr | Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates |
| title_full_unstemmed | Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates |
| title_short | Selective Hydrolysis of Transferrin Promoted by Zr-Substituted Polyoxometalates |
| title_sort | selective hydrolysis of transferrin promoted by zr substituted polyoxometalates |
| topic | polyoxometalate zirconium metalloproteases transferrin hydrolysis |
| url | https://www.mdpi.com/1420-3049/25/15/3472 |
| work_keys_str_mv | AT laurasvanrompuy selectivehydrolysisoftransferrinpromotedbyzrsubstitutedpolyoxometalates AT nadadsavic selectivehydrolysisoftransferrinpromotedbyzrsubstitutedpolyoxometalates AT alvarorodriguez selectivehydrolysisoftransferrinpromotedbyzrsubstitutedpolyoxometalates AT tatjananparacvogt selectivehydrolysisoftransferrinpromotedbyzrsubstitutedpolyoxometalates |