Effect of fluoride toothpastes on enamel demineralization

BACKGROUND: It was the aim of this study to investigate the effect of four different toothpastes with differing fluoride compounds on enamel remineralization. METHODS: A 3 × 3 mm window on the enamel surface of 90 human premolars was demineralized in a hydroxyethylcellulose solution at pH 4.8. The teeth were divided into 6 groups and the lower half of the window was covered with varnish serving as control. The teeth were immersed in a toothpaste slurry containing: placebo tooth paste (group 1); remineralization solution (group 2); Elmex Anticaries (group 3); Elmex Sensitive (group 4); Blend-a-med Complete (group 5) and Colgate GRF (group 6). Ten teeth of each group were used for the determination of the F(- )content in the superficial enamel layer and acid solubility of enamel expressed in soluble phosphorus. Of 6 teeth of each group serial sections were cut and investigated with polarization light microscopy (PLM) and quantitative energy dispersive X-ray analysis (EDX). RESULTS: The PLM results showed an increased remineralization of the lesion body in the Elmex Anticaries, Elmex Sensitive and Colgate GRF group but not in the Blend-a-med group. A statistically significant higher Ca content was found in the Elmex Anticaries group. The fluoride content in the superficial enamel layer was significantly increased in both Elmex groups and the Blend-a-med group. Phosphorus solubility was significantly decreased in both Elmex groups and the Blend-a-med group. CONCLUSION: It can be concluded that amine fluoride compounds in toothpastes result in a clearly marked remineralization of caries like enamel lesions followed by sodium fluoride and sodium monofluorophosphate formulations

Multi-messenger observations of a binary neutron star merger

On 2017 August 17 a binary neutron star coalescence candidate (later designated GW170817) with merger time 12:41:04 UTC was observed through gravitational waves by the Advanced LIGO and Advanced Virgo detectors. The Fermi Gamma-ray Burst Monitor independently detected a gamma-ray burst (GRB 170817A) with a time delay of ~1.7 s with respect to the merger time. From the gravitational-wave signal, the source was initially localized to a sky region of 31 deg2 at a luminosity distance of 40+8-8 Mpc and with component masses consistent with neutron stars. The component masses were later measured to be in the range 0.86 to 2.26 Mo. An extensive observing campaign was launched across the electromagnetic spectrum leading to the discovery of a bright optical transient (SSS17a, now with the IAU identification of AT 2017gfo) in NGC 4993 (at ~40 Mpc) less than 11 hours after the merger by the One- Meter, Two Hemisphere (1M2H) team using the 1 m Swope Telescope. The optical transient was independently detected by multiple teams within an hour. Subsequent observations targeted the object and its environment. Early ultraviolet observations revealed a blue transient that faded within 48 hours. Optical and infrared observations showed a redward evolution over ~10 days. Following early non-detections, X-ray and radio emission were discovered at the transient’s position ~9 and ~16 days, respectively, after the merger. Both the X-ray and radio emission likely arise from a physical process that is distinct from the one that generates the UV/optical/near-infrared emission. No ultra-high-energy gamma-rays and no neutrino candidates consistent with the source were found in follow-up searches. These observations support the hypothesis that GW170817 was produced by the merger of two neutron stars in NGC4993 followed by a short gamma-ray burst (GRB 170817A) and a kilonova/macronova powered by the radioactive decay of r-process nuclei synthesized in the ejecta

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

Binding degeneracy is thought to constitute a fundamental property of the T-cell antigen receptor (TCR), yet its structural basis is poorly understood. We determined the crystal structure of a complex involving the BM3.3 TCR and a peptide (pBM8) bound to the H-2K(bm8) major histocompatibility complex (MHC) molecule, and compared it with the structures of the BM3.3 TCR bound to H-2K(b) molecules loaded with two peptides that had a minimal level of primary sequence identity with pBM8. Our findings provide a refined structural view of the basis of BM3.3 TCR cross-reactivity and a structural explanation for the long-standing paradox that a TCR antigen-binding site can be both specific and degenerate. We also measured the thermodynamic features and biological penalties that incurred during cross-recognition. Our data illustrate the difficulty for a given TCR in adapting to distinct peptide-MHC surfaces while still maintaining affinities that result in functional in vivo responses. Therefore, when induction of protective effector T cells is used as the ultimate criteria for adaptive immunity, TCRs are probably much less degenerate than initially assumed