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Templating metastable Pd2 carboxylate aggregates.

ABSTRACT: Evaluation of the potential for metal-metal (M-M) cooperation to enable catalysis requires access to specific polynuclear aggregates that display appropriate geometry and size. In many cases, exerting synthetic control over the aggregation of simple metal salts is a challenge. For example, Pd(ii) acetate self assembles as a trimer (i.e. Pd3(OAc)6) both in the solid state and in solution and does not feature close Pd-Pd interactions. Related carboxylate-supported Pd2 aggregates (i.e. Pd2(OAc)4), which would feature close Pd-Pd interactions, are thermodynamically metastable in solution phase and thus largely unavailable. Here we demonstrate ion metathesis within pre-formed metal-organic frameworks (MOFs) to prepare metastable Pd2 tetracarboxylates sites. The newly synthesized materials are characterized by elemental analysis, PXRD, SCXRD, EXAFS, XANES, and gas adsorption analysis. In addition, the critical role of network solvation on the kinetics of ion metathesis was revealed by coupled TGA-MS and ICP-MS experiments. The demonstration of templated ion metathesis to generate specific metastable coordination sites that are inaccessible in solution phase chemistry represents a new opportunity to interrogate the chemistry of specific polynuclear metal aggregates.

SUBMITTER: Wang CH

PROVIDER: S-EPMC6369442 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

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Templating metastable Pd2 carboxylate aggregates.

Wang Chen-Hao CH Gao Wen-Yang WY Ma Qing Q Powers David C DC

Chemical science 20181130 6

Evaluation of the potential for metal-metal (M-M) cooperation to enable catalysis requires access to specific polynuclear aggregates that display appropriate geometry and size. In many cases, exerting synthetic control over the aggregation of simple metal salts is a challenge. For example, Pd(ii) acetate self assembles as a trimer (i.e. Pd3(OAc)6) both in the solid state and in solution and does not feature close Pd-Pd interactions. Related carboxylate-supported Pd<s ...[more]

PMID: 30842850

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Project description:Mammalian prion structures and replication mechanisms are poorly understood. Most synthetic recombinant prion protein (rPrP) amyloids prepared without cofactors are non-infectious or much less infectious than bona fide tissue-derived PrPSc. This effect has been associated with differences in folding of the aggregates, manifested in part by reduced solvent exclusion and protease-resistance in rPrP amyloids, especially within residues ~90-160. Substitution of 4 lysines within residues 101-110 of rPrP (central lysine cluster) with alanines (K4A) or asparagines (K4N) allows formation of aggregates with extended proteinase K (PK) resistant cores reminiscent of PrPSc, particularly when seeded with PrPSc. Here we have compared the infectivity of rPrP aggregates made with K4N, K4A or wild-type (WT) rPrP, after seeding with scrapie brain homogenate (ScBH) or normal brain homogenate (NBH). None of these preparations caused clinical disease on first passage into rodents. However, the ScBH-seeded fibrils (only) led to a subclinical pathogenesis as indicated by increases in prion seeding activity, neuropathology, and abnormal PrP in the brain. Seeding activities usually accumulated to much higher levels in animals inoculated with ScBH-seeded fibrils made with the K4N, rather than WT, rPrP molecules. Brain homogenates from subclinical animals induced clinical disease on second passage into "hamsterized" Tg7 mice, with shorter incubation times in animals inoculated with ScBH-seeded K4N rPrP fibrils. On second passage from animals inoculated with ScBH-seeded WT fibrils, we detected an additional PK resistant PrP fragment that was similar to that of bona fide PrPSc. Together these data indicate that both the central lysine cluster and scrapie seeding of rPrP aggregates influence the induction of PrP misfolding, neuropathology and clinical manifestations upon passage in vivo. We confirm that some rPrP aggregates can initiate further aggregation without typical pathogenesis in vivo. We also provide evidence that there is little, if any, biohazard associated with routine RT-QuIC assays.

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Templating metastable Pd2 carboxylate aggregates.

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Templating metastable Pd<sub>2</sub> carboxylate aggregates.

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