A Nanoscale Cobalt Functionalized Strandberg-Type Phosphomolybdate with β-Sheet Conformation Modulation Ability in Anti-Amyloid Protein Misfolding

Abstract

For decades, amyloid β-peptide (Aβ) misfolding aggregates with β-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 Aβ has been regarded as an important anti-amyloid protein misfolding strategy. A polyoxometalate based on {Co(H2O)4}2+ complex and [P2Mo5O23]6− fragments, K8{[Co(H2O)4][HP2Mo5O23]2}·8H2O (abbreviated as CoPM), has been synthesized and structurally characterized using elemental analysis, single-crystal X-ray diffraction (SXRD), IR, UV spectra, bond valence sums (Σs) calculation, and powder XRD (PXRD). CoPM’s primary component, as revealed by structural analysis, is a nanoscale polyoxoanion made of [Co(H2O)4]2+ sandwiched between two [P2Mo5O23]6− pieces. Notably, it is demonstrated that CoPM efficiently modulates Aβ aggregates’ β-sheet-rich conformation.