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Formation mechanisms of hollow manganese hexacyanoferrate particles and construction of a multiple-shell structure.

ABSTRACT: Formation mechanisms of hollow manganese hexacyanoferrate (Mn-HCF) particles have been investigated. Mn-HCF particles, which were precipitated by mixing an aqueous solution of K₃[Fe(CN)₆] with MnCl₂ in the presence of sodium citrate, could be converted into a hollow structure just by washing with distilled water. The powder X-ray diffractometry suggested that the as-prepared particle has a core/shell morphology with different crystal structures: cubic-core and monoclinic-shell. The time evolutions of the particle size and shell thickness indicated that the core was rapidly (but not instantaneously) formed at the initial stage of the precipitation process, followed by a slower shell growth. In addition, the solubility of the cubic core was estimated to be about 2.5 times higher than that of the monoclinic shell, resulting in the preferential dissolution of the interior of the particle by the washing process. The formation procedure has been used to construct multiple-shell hollow Mn-HCF particles containing up to quadruple separated nesting shells by associating an additional growth technique.

SUBMITTER: Shiba F

PROVIDER: S-EPMC8695330 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Formation mechanisms of hollow manganese hexacyanoferrate particles and construction of a multiple-shell structure.

Shiba Fumiyuki F Yamamoto Asumi A Shinta Yuuki Y Mameuda Ushio U Tahara Yuuki Y Okawa Yusuke Y

RSC advances 20210225 15

Formation mechanisms of hollow manganese hexacyanoferrate (Mn-HCF) particles have been investigated. Mn-HCF particles, which were precipitated by mixing an aqueous solution of K3[Fe(CN)6] with MnCl2 in the presence of sodium citrate, could be converted into a hollow structure just by washing with distilled water. The powder X-ray diffractometry suggested that the as-prepared particle has a core/shell morphology with different crystal structures: cubic-core and mo ...[more]

PMID: 35423360

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Project description:Magnetic materials in sample preparation for shotgun phosphoproteomics offer several advantages over conventional systems, as the enrichment can be achieved directly in solution, but they still suffer from some drawbacks, due to limited stability and selectivity, which is supposed to be affected by the hydrophilicity of the polymeric supports used for cation immobilization. The paper describes the development of an improved magnetic material with increased stability, thanks to a two-step covering of the magnetic core, for the enrichment of phosphopeptides in biological samples. Four materials were prepared featuring a polymeric shell with tunable hydrophilicity, obtained by "grafting from" polymerization of glycidyl methacrylate with 0-8.3% of polyethylene glycol methacrylate (PEGMA), the latter used to modulate the hydrophilicity of the material surface. Finally, the materials were functionalized with iminodiacetic acid for Ti4+ ion immobilization. The materials were analyzed for their composition by a combination of CHN elemental analysis and thermogravimetric analysis, also hyphenated to gas chromatography and mass spectrometric detection. Surface characteristics were evaluated by water contact angle measurements, scanning electron microscopy and energy dispersive X-ray spectrometry. These materials were applied to the enrichment of phosphopeptides from yeast protein digests. Peptides were identified by proteomics techniques using nano-high performance liquid chromatography coupled to mass spectrometry and bioinformatics. Qualitatively the peptides identified by the four systems were comparable, with 1606-1693 phosphopeptide identifications and a selectivity of 47-54% for all materials. The physico-chemical features of the identified peptides were also the same for the four materials. In particular, the grand average of hydropathy index values indicated that the enriched phosphopeptides were hydrophilic (ca. 90%), and only some co-enriched non-phosphorylated peptides were hydrophobic (21-28%), regardless of the material used for enrichment. Peptides had a pI ≤ 7, which indicated a well-known bias for acidic peptides binding, attributed to the interaction with the metal center itself. The results indicated that the enrichment of phosphopeptides and the co-enrichment of non-phosphorylated peptides is mainly driven by interactions with Ti4+ and does not depend on the amount of PEGMA chains in the polymer shell.

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Formation mechanisms of hollow manganese hexacyanoferrate particles and construction of a multiple-shell structure.

Publications

Formation mechanisms of hollow manganese hexacyanoferrate particles and construction of a multiple-shell structure.

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