Two mechanisms of oral malodor inhibition by zinc ions

Abstract Objectives The aim of this study was to reveal the mechanisms by which zinc ions inhibit oral malodor. Material and Methods The direct binding of zinc ions to gaseous hydrogen sulfide (H2S) was assessed in comparison with other metal ions. Nine metal chlorides and six metal acetates were examined. To understand the strength of H2S volatilization inhibition, the minimum concentration needed to inhibit H2S volatilization was determined using serial dilution methods. Subsequently, the inhibitory activities of zinc ions on the growth of six oral bacterial strains related to volatile sulfur compound (VSC) production and three strains not related to VSC production were evaluated. Results Aqueous solutions of ZnCl2, CdCl2, CuCl2, (CH3COO)2Zn, (CH3COO)2Cd, (CH3COO)2Cu, and CH3COOAg inhibited H2S volatilization almost entirely. The strengths of H2S volatilization inhibition were in the order Ag+ > Cd2+ > Cu2+ > Zn2+. The effect of zinc ions on the growth of oral bacteria was strain-dependent. Fusobacterium nucleatum ATCC 25586 was the most sensitive, as it was suppressed by medium containing 0.001% zinc ions. Conclusions Zinc ions have an inhibitory effect on oral malodor involving the two mechanisms of direct binding with gaseous H2S and suppressing the growth of VSC-producing oral bacteria.

PDLLA scaffolds with Cu- and Zn-doped bioactive glasses having multifunctional properties for bone regeneration.

Novel multifunctional scaffolds for bone regeneration can be developed by incorporation of bioactive glasses (BG) doped with therapeutic and antibacterial metal ions, such as copper (Cu) and zinc (Zn), into a biodegradable polymer. In this context, porous composite materials of biodegradable poly(d, l-lactide) (PDLLA) mixed with sol-gel BG of chemical composition 60SiO2 ; 25CaO; 11Na2 O; and 4P2 O5 (mol %) doped with either 1 mol % of CuO or ZnO, and with both metals, were prepared. The cytocompatibility of the scaffolds on bone marrow stromal cells (ST-2) depended on both, the amount of glass filler and the concentration of metal ion, as evaluated by lactate dehydrogenase (LDH) activity, cell viability (water-soluble tetrazolium salt [WST-8]), and by cell morphology (scanning electron microscopy [SEM]) tests. In particular, scaffolds having a filler content of 10 wt % showed the highest cytocompatibility. In addition, compared to the neat polymer, the scaffolds containing Cu promoted the angiogenesis marker (Vascular endothelial growth factor concentration) to a larger extent while scaffolds containing Zn increased the osteogenesis marker (specific alkaline phosphatase-activity). Noteworthy, the scaffolds with both metal ions showed a combined effect on both properties. Cu- and Zn-doped glasses also provided higher antibacterial capacity to PDLLA-based scaffolds against methicillin-resistant S. aureus bacteria than undoped glass. In combination, our results showed that by a proper addition of Cu- and Zn-doped BG to a PDLLA matrix, multifunctional composite scaffolds with enhanced biological activity can be designed for bone tissue regeneration. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 746-756, 2017.

Functional and structural studies of a Phospholipase A2-like protein complexed to zinc ions: Insights on its myotoxicity and inhibition mechanism.

BACKGROUND: One of the main challenges in snakebite envenomation treatment is the development of stable, versatile and efficient anti-venom therapies. Local myotoxicity in accidents involving snakes from the Bothrops genus is still a consequence of serum therapy inefficient neutralization that may lead to permanent sequelae in their victims. One of the classes of toxins that participate in muscle necrosis is the PLA2-like proteins. The aim of this work was to investigate the role of zinc ions in the inhibition of PLA2-like proteins and to advance the current knowledge of their action mechanism. METHODS: Myographic and electrophysiological techniques were used to evaluate the inhibitory effect of zinc ions, isothermal titration calorimetry assays were used to measure the affinity between zinc ions and the toxin and X-ray crystallography was used to reveal details of this interaction. RESULTS: We demonstrated that zinc ions can effectively inhibit the toxin by the interaction with two different sites, which are related to two different mechanism of inhibition: preventing membrane disruption and impairing the toxin state transition. Furthermore, structural study presented here included an additional step in the current myotoxic mechanism improving the comprehension of the allosteric transition that PLA2-like proteins undergo to exert their function. CONCLUSIONS: Our findings show that zinc ions are inhibitors of PLA2-like proteins and suggest two different mechanisms of inhibition for these ions. GENERAL SIGNIFICANCE: Zinc is a new candidate that can assist in anti-venom treatments and can promote the design of new and even more accurate structure-based inhibitors for PLA2-like proteins.

A simple strategy for the purification of native recombinant full-length human RPL10 protein from inclusion bodies.

The L10 ribosomal protein (RPL10) plays a role in the binding of the 60 S and 40 S ribosomal subunits and in mRNA translation. The evidence indicates that RPL10 also has multiple extra-ribosomal functions, including tumor suppression. Recently, the presence of RPL10 in prostate and ovarian cancers was evaluated, and it was demonstrated to be associated with autistic disorders and premature ovarian failure. In the present work, we successfully cloned and expressed full-length human RPL10 (hRPL10) protein and isolated inclusion bodies containing this protein that had formed under mild growth conditions. The culture produced 376mg of hRPL10 protein per liter of induced bacterial culture, of which 102.4mg was present in the soluble fraction, and 25.6mg was recovered at approximately 94% purity. These results were obtained using a two-step process of non-denaturing protein extraction from pelleted inclusion bodies. We studied the characteristics of this protein using circular dichroism spectroscopy and by monitoring the changes induced by the presence or absence of zinc ions using fluorescence spectrometry. The results demonstrated that the protein obtained using these non-conventional methods retained its secondary and tertiary structure. The conformational changes induced by the incorporation of zinc suggested that this protein could interact with Jun or the SH3 domain of c-yes. The results suggested that the strategy used to obtain hRPL10 is simple and could be applied to obtaining other proteins that are susceptible to degradation.