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Bonding Potential (bonding + potential)
Selected AbstractsFour-year water degradation of a resin-modified glass-ionomer adhesive bonded to dentinEUROPEAN JOURNAL OF ORAL SCIENCES, Issue 1 2004Jan De Munck Glass-ionomers are auto-adhesive to tooth tissue through combined micro-mechanical and chemical bonding. How much each of the two bonding components contributes to the actual bonding effectiveness is, however, not known and there is not much information available on long-term stability. The objective of this study was to assess the bonding effectiveness of a resin-modified glass-ionomer adhesive to dentin after 4 yr of water storage. Fuji Bond LC (GC) was applied without (i) and with pretreatment using (ii) a polyalkenoic acid conditioner and (iii) a 37.5% phosphoric acid etchant. The etchant was used to exclude any chemical interaction with hydroxyapatite. The micro-tensile bond strength (µTBS) to dentin decreased significantly over the 4 yr period in all three experimental groups. After 24 h and 4 yr, the lowest µTBS was recorded when dentin was not pretreated. The highest µTBS was obtained following polyalkenoic acid pretreatment, although this was not significantly different from specimens that were pretreated using phosphoric acid. Pretreating dentin with phosphoric acid intensified micromechanical interlocking at the expense of chemical bonding potential to hydroxyapatite. Nevertheless, correlating the µTBS data with failure analysis through scanning electron microscopy and transmission electron microscopy indicated that combined micro-mechanical and chemical bonding involving pretreatment with the polyalkenoic acid conditioner yielded the most durable bond. [source] Different mechanisms influencing permeation of PDGF-AA and PDGF-BB across the blood,brain barrierJOURNAL OF NEUROCHEMISTRY, Issue 1 2003Abba J. Kastin Abstract Platelet-derived growth factor (PDGF) exerts neurotrophic and neuromodulatory effects on the CNS. To determine the permeability of the blood,brain barrier (BBB) to PDGF, we examined the blood-to-brain influx of radioactively labeled PDGF isoforms (PDGF-AA and PDGF-BB) by multiple-time regression analysis after intravenous (i.v.) injection and by in-situ perfusion, and also determined the physicochemical characteristics which affect their permeation across the BBB, including lipophilicity (measured by octanol:buffer partition coefficient), hydrogen bonding (measured by differences in octanol : buffer and isooctane : buffer partition coefficients), serum protein binding (measured by capillary electrophoresis), and stability of PDGF in blood 10 min after i.v. injection (measured by HPLC). After i.v. bolus injection, neither 125I-PDGF-AA nor 125I-PDGF-BB crossed the BBB, their influx rates being similar to that of the vascular marker 99mTc-albumin. 125I-PDGF-AA degraded significantly faster in blood than 125I-PDGF-BB. PDGF-BB, however, was completely bound to a large protein in serum whereas PDGF-AA showed no binding. Thus, degradation might explain the poor blood-to-brain influx of PDGF-AA, whereas protein binding could explain the poor influx of circulating PDGF-BB. Despite their lack of permeation in the intact mouse, both 125I-PDGF-AA and 125I-PDGF-BB entered the brain by perfusion in blood-free buffer, and the significantly faster rate of 125I-PDGF-AA than 125I-PDGF-BB may be explained by the lower hydrogen bonding potential of 125I-PDGF-AA. Thus, the lack of significant distribution of PDGF from blood to brain is not because of the intrinsic barrier function of the BBB but probably because of degradation and protein binding. Information from these studies could be useful in the design of analogues for delivery of PDGF as a therapeutic agent. [source] Anisotropic surface chemistry of aspirin crystalsJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 8 2007Jerry Y.Y. Heng Abstract The wettability of the (001), (100), and (011) crystallographic facets of macroscopic aspirin crystals has been experimentally investigated using a sessile drop contact angle (,) method. , for a nonpolar liquid was very similar for all three facets, though significant , differences were observed for three polar probe liquids. The observed hydrophobicity of the (001) and (100) facets is ascribed to a reduced hydrogen bonding potential at these surfaces, whilst the observed hydrophilicity of facet (011) may be attributed to presence of surface carboxylic functionalities as confirmed by X-ray photoelectron spectroscopy (XPS). The dispersive component of the surface free energy (,) was similar for all three facets (35,±,2 mJ/m2). The total surface energy, ,s varied between 46 and 60 mJ/m2 due to significant variations in the polar/acid,base components of , for all facets. Surface polarity as determined by , measurements and XPS data were in good agreement, linking the variations in wettability to the concentration of oxygen containing surface functional groups. In conclusion, the wettability and the surface energy of a crystalline organic solid, such as aspirin, was found to be anisotropic and facet dependant, and in this case, related to the presence of surface carboxylic functionalities. © 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96:2134,2144, 2007 [source] Determination of dissociation energy for ligand exchange reaction from EXAFSJOURNAL OF SYNCHROTRON RADIATION, Issue 2 2001T. Miyanaga EXAFS (extended X-ray absorption fine structure) experiments were performed at several different temperatures for a series of 3d transition metal ions (Cr3+, Fe3+, Fe2+, Ni2+, Co2+, Zn2+) in aqueous solutions. Anharmonic EXAFS analyses, which include up to third order cumulant, were carried out to study on the metal-oxygen bonding potential. According to the model in which the dissociation process is dominant for the ligand-water exchange reaction, the dissociation energy has been first evaluated from EXAFS in solution phase. [source] Change in dimerization mode by removal of a single unsatisfied polar residue located at the interfacePROTEIN SCIENCE, Issue 9 2000P. R. Pokkuluri Abstract The importance of unsatisfied hydrogen bonding potential on protein-protein interaction was studied. Two alternate modes of dimerization (conventional and flipped form) of an immunoglobulin light chain variable domain (VL) were previously identified. In the flipped form, interface residue Gln89 would have an unsatisfied hydrogen bonding potential. Removal of this Gln should render the flipped dimer as the more favorable quaternary form. High resolution crystallographic studies of the Q89A and Q89L mutants show, as we predicted, that these proteins indeed form flipped dimers with very similar interfaces. A small cavity is present in the Q89A mutant that is reflected in the ,100 times lower association constant than found for the Q89L mutant. The association constant of Q89A and Q89L proteins (4 × 106 M,1 and > 108 M,1) are 10- and 1,000-fold higher than that of the wild-type protein that forms conventional dimers clearly showing the energetic reasons for the flipped dimer formation. [source] | ||||||||||