Alterations promoted by acid straightening and/or bleaching in hair microstructures.

Human hair is a biopolymer constituted mainly of keratin intermediate filaments, lipids, pigments and water. Cosmetic treatments usually interact with the hair at the molecular level, inducing changes in its components and modifying the physicochemical and mechanical properties of the fibers. Here, the effect of acid straightening on the morphology and ultrastructure of Caucasian hair was investigated by a group of complementary experimental methods: wide-, small- and ultra-small-angle X-ray scattering; high-resolution 3D X-ray microscopy; quasi-elastic neutron scattering and inelastic neutron scattering; thermogravimetry-mass spectrometry; and differential scanning calorimetry (DSC). X-ray diffraction patterns showed that acid straightening associated with a flat iron (∼180°C) changed the cortex of the fiber, shown by denaturation of the intermediate filaments (measured by DSC). The increase in the spacing of the lipid layers and the observation of the dehydration behavior of the fiber provided indications that water may be confined between these layers, while neutron spectroscopy showed alterations in the vibration mode of the CH2 groups of the lipids and an increase of the proton (H+) mobility in the hair structure. The latter may be associated with the extremely low pH of the formulation (pH ≃ 1). Additionally, this investigation showed that bleached hair (one-time bleached) is more damaged by the action of acid straightening than virgin hair, which was shown by a threefold increase in the percentage of total porosity of the tresses. The obtained results demonstrate that the investigation approach proposed here can provide very important thermodynamic and structural information on induced changes of hair structure, and certainly can be applied for the evaluation of the action mode and efficiency of cosmetic treatments.

The development of new oral vaccines using porous silica.

Ordered mesoporous silica (OMS) was proved to be an efficient oral adjuvant capable to deliver a wide in size variety of different antigens, promoting efficient immunogenicity. This material can be used in single or polivalent vaccines, which have been developed by a group of Brazilian scientists. The experiments performed with the model protein Bovine Serum Albumin (BSA) gave the first promissing results, that were also achieved by testing the virus like particle surface antigen of hepatitis B (HBsAg) and diphtheria anatoxin (dANA). Nanostructured OMS, SBA-15 type, with bi-dimensional hexagonal porous symmetry was used to encapsulate the antigens either in the mesoporous (pore diameter ∼ 10 nm) or macroporous (pore diameter > 50 nm) regions. This silica vehicle proved to be capable to create an inflammatory response, did not exhibit toxicity, being effective to induce immunity in high and low responder mice towards antibody production. The silica particles are in the range of micrometer size, leaving no trace in mice organs due to its easy expulsion by faeces. The methods of physics, usually employed to characterize the structure, composition and morphology of materials are of fundamental importance to develop proper oral vaccines in order to state the ideal antigen load to avoid clustering and to determine the rate of antigen release in different media mimicking body fluids.

Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions.

Hepatitis B virus causes acute and chronic infections in millions of people worldwide and, since 1982, a vaccine with 95% effectiveness has been available for immunization. The main component of the recombinant hepatitis B vaccine is the surface antigen protein (HBsAg). In this work, the effect of pH, ionic strength and temperature on the native state of the HBsAg antigen were studied by a combination of biophysical methods that included small angle X-ray scattering, synchrotron radiation circular dichroism, fluorescence and surface plasmon resonance spectroscopies, as well as in vivo and in vitro potency assays. The native conformation, morphology, radius of gyration, and antigenic properties of the HBsAg antigen demonstrate high stability to pH treatment, especially in the pH range employed in all stages of HBsAg vaccine production and storage. The HBsAg protein presents thermal melting point close to 56 °C, reaching a more unfolded state after crossing this point, but it only experiences loss of vaccine potency and antigenic properties at 100 °C. Interestingly, a 6-month storage period does not affect vaccine stability, and the results are similar when the protein is kept under refrigerated conditions or at room temperature (20 °C). At frozen temperatures, large aggregates (>200 nm) are formed and possibly cause loss of HBsAg content, but that does not affect the in vivo assay. Furthermore, HBsAg has a well-ordered secondary structure content that is not affected when the protein is formulated with silica SBA-15, targeting the oral delivery of the vaccine. The combined results from all the characterization techniques employed in this study showed the high stability of the antigen at different storage temperature and extreme values of pH. These findings are important for considering the delivery of HBsAg to the immune system via an oral vaccine.

Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions

Hepatitis B virus causes acute and chronic infections in millions of people worldwide and, since 1982, a vaccine with 95% effectiveness has been available for immunization. The main component of the recombinant hepatitis B vaccine is the surface antigen protein (HBsAg). In this work, the effect of pH, ionic strength and temperature on the native state of the HBsAg antigen were studied by a combination of biophysical methods that included small angle X-ray scattering, synchrotron radiation circular dichroism, fluorescence and surface plasmon resonance spectroscopies, as well as in vivo and in vitro potency assays. The native conformation, morphology, radius of gyration, and antigenic properties of the HBsAg antigen demonstrate high stability to pH treatment, especially in the pH range employed in all stages of HBsAg vaccine production and storage. The HBsAg protein presents thermal melting point close to 56°C, reaching a more unfolded state after crossing this point, but it only experiences loss of vaccine potency and antigenic properties at 100°C. Interestingly, a 6-month storage period does not affect vaccine stability, and the results are similar when the protein is kept under refrigerated conditions or at room temperature (20°C). At frozen temperatures, large aggregates (>200nm) are formed and possibly cause loss of HBsAg content, but that does not affect the in vivo assay. Furthermore, HBsAg has a well-ordered secondary structure content that is not affected when the protein is formulated with silica SBA-15, targeting the oral delivery of the vaccine. The combined results from all the characterization techniques employed in this study showed the high stability of the antigen at different storage temperature and extreme values of pH. These findings are important for considering the delivery of HBsAg to the immune system via an oral vaccine.

Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions

Hepatitis B virus causes acute and chronic infections in millions of people worldwide and, since 1982, a vaccine with 95% effectiveness has been available for immunization. The main component of the recombinant hepatitis B vaccine is the surface antigen protein (HBsAg). In this work, the effect of pH, ionic strength and temperature on the native state of the HBsAg antigen were studied by a combination of biophysical methods that included small angle X-ray scattering, synchrotron radiation circular dichroism, fluorescence and surface plasmon resonance spectroscopies, as well as in vivo and in vitro potency assays. The native conformation, morphology, radius of gyration, and antigenic properties of the HBsAg antigen demonstrate high stability to pH treatment, especially in the pH range employed in all stages of HBsAg vaccine production and storage. The HBsAg protein presents thermal melting point close to 56°C, reaching a more unfolded state after crossing this point, but it only experiences loss of vaccine potency and antigenic properties at 100°C. Interestingly, a 6-month storage period does not affect vaccine stability, and the results are similar when the protein is kept under refrigerated conditions or at room temperature (20°C). At frozen temperatures, large aggregates (>200nm) are formed and possibly cause loss of HBsAg content, but that does not affect the in vivo assay. Furthermore, HBsAg has a well-ordered secondary structure content that is not affected when the protein is formulated with silica SBA-15, targeting the oral delivery of the vaccine. The combined results from all the characterization techniques employed in this study showed the high stability of the antigen at different storage temperature and extreme values of pH. These findings are important for considering the delivery of HBsAg to the immune system via an oral vaccine.

Probing Water Mobility in Human Dentine with Neutron Spectroscopy.

The aim of this study was to investigate hydrogen mobility within innate and demineralized human dentine. Dentine sections from extracted human molars, demineralized or not, were analyzed by combining neutron spectroscopy with thermal analysis. For the thermal analysis of the samples, differential scanning calorimetry and thermal gravimetric analysis, coupled with Fourier transform infrared spectroscopy, were performed. The hydrogen dynamics of water, collagen, and hydroxyl groups present in the samples were investigated via neutron spectroscopy. From the mass loss observed from the thermogravimetric analysis curves up to 600 °C, the same amount of organic content is identified in the samples. From the differential scanning calorimetry curves, a higher change in enthalpy associated with the denaturation of collagen is registered in the demineralized dentine; that is, a structural change occurs in the collagen subsequent to demineralization. Since the intensity measured by neutron spectroscopy is dominated by the signal from hydrogen, in our samples-coming mostly from the bulk-like and loosely bound water as well as from the collagen itself-higher proton mobility within the demineralized dentine was detected when compared with innate dentine. In the demineralized dentine, this proton mobility amounts to 80%, while the remaining hydrogen accounts for a combination of 1) structural hydroxyls, as a result of the incomplete dissolution of the mineral phase by acid etching, and 2) hydrogen tightly bound in the collagen structure. By combining neutron spectroscopy with the calorimetry data, our findings support the idea that hydroxyapatite protects the collagen in innate dentine. Demineralized dentine, however, acts as a sponge where free bulk-like water is trapped.

Conceptual design of the time-of-flight backscattering spectrometer, MIRACLES, at the European Spallation Source.

In this work, we present the conceptual design of the backscattering time-of-flight spectrometer MIRACLES approved for construction at the long-pulse European Spallation Source (ESS). MIRACLES's unparalleled combination of variable resolution, high flux, extended energy, and momentum transfer (0.2-6 Å(-1)) ranges will open new avenues for neutron backscattering spectroscopy. Its remarkable flexibility can be attributed to 3 key elements: the long-pulse time structure and low repetition rate of the ESS neutron source, the chopper cascade that tailors the moderator pulse in the primary part of the spectrometer, and the bent Si(111) analyzer crystals arranged in a near-backscattering geometry in the secondary part of the spectrometer. Analytical calculations combined with instrument Monte-Carlo simulations show that the instrument will provide a variable elastic energy resolution, δ(h ω), between 2 and 32 µeV, when using a wavelength of λ ≈ 6.267 Å (Si(111)-reflection), with an energy transfer range, h ω, centered at the elastic line from -600 to +600 µeV. In addition, when selecting λ ≈ 2.08 Å (i.e., the Si(333)-reflection), δ(h ω) can be relaxed to 300 µeV and h ω from about 10 meV in energy gain to ca -40 meV in energy loss. Finally, the dynamic wavelength range of MIRACLES, approximately 1.8 Å, can be shifted within the interval of 2-20 Å to allow the measurement of low-energy inelastic excitations.

Photoluminescence and optical absorption of Cs2NaScF6:Cr3+.

The main objective of this paper is the characterization of the spectroscopic properties of new materials that are prospective laser media. This approach allows for the comparison of the properties of the Cr3+ in different environments. Here, we have studied the photoluminescence and optical absorption of Cs2NaScF6:Cr3+ single crystals. On the basis of near-infrared luminescence measurements at 2, 77, and 300 K the observed lines originated from the Cr3+-centres were associated with the 4T2(4F) --> 4A2(4F) transition and the lifetimes were obtained. In spite of the quenching observed as a function of temperature at least 10% of the 2 K emission intensity for Cs2NaScF6 doped with 1% of Cr3+ remains at room temperature. Besides, the 2 K emission broad band could be well described in terms of normal modes of the octahedral complex [CrF6]3-, and the Racah and crystal-field parameters calculated.

Quasi-elastic neutron scattering study of dimethyl-sulfoxide-water mixtures: probing molecular mobility in a nonideal solution.

The translational and rotational motions of water and dimethyl sulfoxide, [DMSO, (CH(3))(2)SO] have been investigated using quasi-elastic neutron scattering. Water-DMSO mixtures at five DMSO mole fractions, chi(DMSO), ranging from 0 to 0.75, were measured. Hydrogen-deuterium substitution was used to extract independently the water proton dynamics (d-DMSO-H(2)O), the DMSO methyl proton dynamics (h-DMSO-D(2)O) and to obtain background corrections (d-DMSO-D(2)O). The translational diffusion of water slows down significantly compared to bulk water at all chi(DMSO)>0. The rotational time constant for water exhibits a maximum at chi(DMSO)=0.33 that corresponds to the observed maximum of the viscosity of the mixture. Data for DMSO can be analyzed in terms of a relatively slow tumbling of the molecule about its center-of-mass in conjunction with random translational diffusion. The rotational time constant for this motion exhibits some dependence on chi(DMSO), while the translational diffusion constant shows no clear variation for chi(DMSO)>0. The results presented reinforce the idea that due to the stronger associative nature of DMSO, DMSO-water aggregates are formed over the whole composition range, disturbing the tetrahedral natural arrangement of the water molecules. As a consequence adding DMSO to water causes a drastic slowing down of the dynamics of the water molecule, and vice versa.

Glass transition in the polaron dynamics of colossal magnetoresistive manganites.

Neutron scattering measurements on a bilayer manganite near optimal doping show that the short-range polaron correlations are completely dynamic at high T, but then freeze upon cooling to a temperature T(*) approximately equal 310 K. This glass transition suggests that the paramagnetic/insulating state arises from an inherent orbital frustration that inhibits the formation of a long-range orbital- and charge-ordered state. Upon further cooling into the ferromagnetic-metallic state (T(C) = 114 K), where the polarons melt, the diffuse scattering quickly develops into a propagating, transverse optic phonon.