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This study presents evidence at molecular level for the chemical interaction between human dentin from different tooth regions and a monomer with phosphate groups, incorporated in the formulation of a simplified adhesive system. Because dentin was observed as a powder, previous verification was obtained for an eventual collagen denaturation due to the grinding process. The presence of chemical bonds involving coronal (CD) or radicular dentin (RD) was investigated using multinuclear magnetic resonance (MR) techniques. Narrow signals were identified in the carbon magic angle spinning (MAS) spectra of CD and RD treated with the adhesive, which were assigned to methylenic groups in methacryloyloxydecyl dihydrogen phosphate (MDP) bound to hydroxyapatite Ca2+; 1H spectra of the adhesive components and treated dentin, in ethanol, support this conclusion. (31)P MAS spectra obtained from both dentin regions present additional shielding and broadening effects subsequent to application and photopolymerization of the adhesive, which were higher for CD. Multinuclear MR studies provided evidence for the interaction of the adhesive with dentin, which involves hydroxyapatite and is stronger for CD than for RD, but no direct proof was obtained on bonding to collagen.
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http://dx.doi.org/10.1007/s10856-007-3148-9 | DOI Listing |
Inorg Chem
September 2025
School of Science, Constructor University, Campus Ring 1, 28759 Bremen, Germany.
We report on the synthesis, functionalization, and structural characterization of 11 novel dimethylarsinate-functionalized arsenomolybdates(V), [RAsMoO(OH){AsO(CH)}] (R = HO, CH, CH, CH, 3,5-(HOOC)CH, 4-FCH, 4-FCCH, 4-FCOCH, 4-BrCH, and 4-NCH) and [AsMoO(OH){AsO(CH)}], featuring a reduced hexanuclear {MoO} core, peripherally coordinated by three dimethylarsinate ligands and centrally functionalized with diverse organoarsonate, arsenate, or arsenite groups, including carboxylated, fluorinated, brominated, and azido derivatives. Synthesized via a simple one-pot aqueous method, the compounds were thoroughly characterized by single-crystal X-ray diffraction, thermogravimetric analysis, and elemental analysis in the solid state. Solution-phase stability was assessed by multinuclear (H, C, and F) nuclear magnetic resonance, while gas-phase behavior and fragmentation pathways were probed through electrospray ionization mass spectrometry, and tandem mass spectrometry (collision-induced dissociation).
View Article and Find Full Text PDFJ Am Chem Soc
September 2025
State Key Laboratory of Applied Organic Chemistry, College of Chemistry and Chemical Engineering, Lanzhou Magnetic Resonance Center, Lanzhou University, Lanzhou, Gansu 730000, China.
Further advancement in the research area of covalent organic frameworks (COFs) is in urgent need of structural information with high accuracy. The bottleneck in characterization is the lack of effective strategies to resolve the complex features (e.g.
View Article and Find Full Text PDFJ Phys Chem Lett
August 2025
Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.
Quadrupolar spin resonance (QSR) is radio frequency spectroscopy that provides a chemical fingerprint in the absence of a magnetic field. Materials may present QSR spectra featuring multiple overlapping isotopic resonances, leading to ambiguous spectral assignments. We show how the application of a weak magnetic field (≤50 mT) enables measurement of the nuclear gyromagnetic ratio associated with each resonance with sufficient precision for isotopic identification.
View Article and Find Full Text PDFUnderstanding protein structures and their interactions within natural cellular environments is essential for deciphering cellular processes and advancing therapeutic development. Obtaining atomic-level information about protein structural changes in cellular contexts poses a significant challenge. Here, we introduce a F-based, H-assisted dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR approach that offers exceptionally high sensitivity and specificity, enabling background-free detection of target proteins in mammalian cells for atomic-level structural analysis.
View Article and Find Full Text PDFJ Am Chem Soc
August 2025
Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States.
Understanding protein structures and their interactions within natural cellular environments is essential for deciphering cellular processes and advancing therapeutic development. Obtaining atomic-level information about protein structural changes in cellular contexts poses a significant challenge. Here, we introduce a F-based, H-assisted dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR approach that offers exceptionally high sensitivity and specificity, enabling background-free detection of target proteins in mammalian cells for atomic-level structural analysis.
View Article and Find Full Text PDF