Citation: Ji-Ai HUA, Xue-Man WEI, Na ZHANG, Peng-Ju CHEN, Xiang MA. Synthesis of a Linear Cobalt-Substituted Strandberg-Type Polyphospolybdate with Ability in Modulating Conformation of Aβ-Peptide Misfolding Aggregation[J]. Chinese Journal of Inorganic Chemistry, ;2022, 38(10): 1908-1918. doi: 10.11862/CJIC.2022.207 shu

Synthesis of a Linear Cobalt-Substituted Strandberg-Type Polyphospolybdate with Ability in Modulating Conformation of Aβ-Peptide Misfolding Aggregation

Ji-Ai HUA ^{1, #,,} ,
Xue-Man WEI ^{2, #} ,
Na ZHANG ³ ,
Peng-Ju CHEN ¹ ,
Xiang MA ^{3, 4,,}

1.
Chemistry and Chemical Engineering Department, Taiyuan Institute of Technology, Taiyuan 030008, China
2.
Department of Geriatrics, First affiliated Hospital of Naval Medical University, Shanghai 200081, China
3.
Laboratory of Biochemistry and Pharmacy, Taiyuan Institute of Technology, Taiyuan 030008, China
4.
State Key Laboratory of Coordination Chemistry, Nanjing University, Nanjing 210023, China

Corresponding author: Ji-Ai HUA, jiaihua01660@163.com Xiang MA, maxiang@tit.edu.cn
Received Date: 21 March 2022
Revised Date: 23 August 2022

Figures(9)

A linear Co-substituted Strandberg-type polyphosphomolybdate (H₂en)₆{[Co(H₂O)₄] (P₂ Mo₅O₂₃)}₃·11H₂O (abbreviated as CoPM, en=ethylenediamine) has been synthesized and structurally characterized by elemental analyses, IR spectrum, thermogravimetric analysis, and single-crystal X-ray diffraction. Structural analysis reveals that the molecular structural unit of CoPM consists of [P₂Mo₅O₂₃]^6- cluster, and Co-complex [Co(H ₂O)₄]²⁺, and they join alternately to form the 1D infinite extension skeleton of CoPM. Furthermore, each cyclic unit of the CoPM chain contains three {[Co(H₂O)₄](P₂Mo₅O₂₃)}^4- units in solid states based on bond valence sums (BVS) calculation. The intervention of CoPM on the misfolding process of amyloid β-protein (Aβ) was studied by the thioflavin T fluorescence method, turbidimetric method, circular dichroism, and NMR. The results indicate that CoPM can modulate the β-sheet-rich conformation of Aβ aggregates, and thus reduce the formation of toxic species. Moreover, 2', 7'-dichlorofluorescein (DCF) fluorescence and cytotoxicity experiments showed that CoPM could also eliminate reactive oxygen species (ROS) produced by Cu²⁺-Aβ aggregates. It can inhibit the cytotoxicity of β-sheet-rich species and protect synapses of PC12 cells.
- polyphosphomolybdate,
- anti-oxidation,
- conformation modulation,
- protein-misfolding disease,
- amyloid β-peptide
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