A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding
For decades, amyloid <i>β</i>-peptide (A<i>β</i>) misfolding aggregates with <i>β</i>-sheet structures have been linked to the occurrence and advancement of Alzheimer’s disease (AD) development and progression. As a result, modulating the misfolding mode of A<i...
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MDPI AG
2023-11-01
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author | Man Wang Jiai Hua Pei Zheng Yuanzhi Tian Shaodan Kang Junjun Chen Yifan Duan Xiang Ma |
author_facet | Man Wang Jiai Hua Pei Zheng Yuanzhi Tian Shaodan Kang Junjun Chen Yifan Duan Xiang Ma |
author_sort | Man Wang |
collection | DOAJ |
description | For decades, amyloid <i>β</i>-peptide (A<i>β</i>) misfolding aggregates with <i>β</i>-sheet structures have been linked to the occurrence and advancement of Alzheimer’s disease (AD) development and progression. As a result, modulating the misfolding mode of A<i>β</i> has been regarded as an important anti-amyloid protein misfolding strategy. A polyoxometalate based on {Co(H<sub>2</sub>O)<sub>4</sub>}<sup>2+</sup> complex and [P<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sup>6−</sup> fragments, K<sub>8</sub>{[Co(H<sub>2</sub>O)<sub>4</sub>][HP<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sub>2</sub>}·8H<sub>2</sub>O (abbreviated as CoPM), has been synthesized and structurally characterized using elemental analysis, single-crystal X-ray diffraction (SXRD), IR, UV spectra, bond valence sums (Σ<i>s</i>) calculation, and powder XRD (PXRD). CoPM’s primary component, as revealed by structural analysis, is a nanoscale polyoxoanion made of [Co(H<sub>2</sub>O)<sub>4</sub>]<sup>2+</sup> sandwiched between two [P<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sup>6−</sup> pieces. Notably, it is demonstrated that CoPM efficiently modulates A<i>β</i> aggregates’ <i>β</i>-sheet-rich conformation. |
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spelling | doaj.art-1ff6a27b978041bc808316d5dc1dbca92023-11-24T14:48:29ZengMDPI AGInorganics2304-67402023-11-01111144210.3390/inorganics11110442A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein MisfoldingMan Wang0Jiai Hua1Pei Zheng2Yuanzhi Tian3Shaodan Kang4Junjun Chen5Yifan Duan6Xiang Ma7Chemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaChemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaChemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaLaboratory of Biochemistry and Pharmacy, Taiyuan Institute of Technology, Taiyuan 030008, ChinaChemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaChemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaLaboratory of Biochemistry and Pharmacy, Taiyuan Institute of Technology, Taiyuan 030008, ChinaChemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, ChinaFor decades, amyloid <i>β</i>-peptide (A<i>β</i>) misfolding aggregates with <i>β</i>-sheet structures have been linked to the occurrence and advancement of Alzheimer’s disease (AD) development and progression. As a result, modulating the misfolding mode of A<i>β</i> has been regarded as an important anti-amyloid protein misfolding strategy. A polyoxometalate based on {Co(H<sub>2</sub>O)<sub>4</sub>}<sup>2+</sup> complex and [P<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sup>6−</sup> fragments, K<sub>8</sub>{[Co(H<sub>2</sub>O)<sub>4</sub>][HP<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sub>2</sub>}·8H<sub>2</sub>O (abbreviated as CoPM), has been synthesized and structurally characterized using elemental analysis, single-crystal X-ray diffraction (SXRD), IR, UV spectra, bond valence sums (Σ<i>s</i>) calculation, and powder XRD (PXRD). CoPM’s primary component, as revealed by structural analysis, is a nanoscale polyoxoanion made of [Co(H<sub>2</sub>O)<sub>4</sub>]<sup>2+</sup> sandwiched between two [P<sub>2</sub>Mo<sub>5</sub>O<sub>23</sub>]<sup>6−</sup> pieces. Notably, it is demonstrated that CoPM efficiently modulates A<i>β</i> aggregates’ <i>β</i>-sheet-rich conformation.https://www.mdpi.com/2304-6740/11/11/442strandberg-type polyoxometalateamyloid protein misfoldingconformation modulationcobalt complexes |
spellingShingle | Man Wang Jiai Hua Pei Zheng Yuanzhi Tian Shaodan Kang Junjun Chen Yifan Duan Xiang Ma A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding Inorganics strandberg-type polyoxometalate amyloid protein misfolding conformation modulation cobalt complexes |
title | A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding |
title_full | A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding |
title_fullStr | A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding |
title_full_unstemmed | A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding |
title_short | A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with <i>β</i>-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding |
title_sort | nanoscale cobalt functionalized strandberg type phosphomolybdate with i β i sheet conformation modulation ability in anti amyloid protein misfolding |
topic | strandberg-type polyoxometalate amyloid protein misfolding conformation modulation cobalt complexes |
url | https://www.mdpi.com/2304-6740/11/11/442 |
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