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.

The development of new oral vaccines using porous silica

Ordered mesoporous silica 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 ordered mesoporous silica, 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.

Magnetic, structural and cation distribution studies on [Formula: see text] (x = 0.00, 0.02, 0.04, 0.06 and 0.1) nanoparticles.

We synthesized and characterized the colloidal suspensions of [Formula: see text] nanoparticles with x = 0.00, 0.02, 0.04, 0.06 and 0.1. The effect of the Fe3+ ion replacement by Nd3+ on the crystal structure is in-depth studied. The samples were characterized by the following techniques: X-ray diffraction (XRD), UV-Vis spectrophotometry, transmission electronic microscopy (TEM), small-angle X-ray scattering (SAXS), magnetization as a function of applied magnetic field (M-H loops) and magnetization as a function of temperature in zero-field-cooled and field-cooled regimes (ZFC-FC). From XRD cation distribution, structural parameters were extracted. The increasing in the bandgap is interpreted as a result of the higher interatomic separation with the doping. TEM micrographs reveal a polydisperse size and shape distribution of particles. The results for the volume-weighted average diameter measured by SAXS are consistent with those determined by XRD. From the M-H loops we found that the superparamagnetic (SPM) regime contributes with 95-97% for all samples, while only 3-5% contribution comes from the paramagnetic (PM) regime. The saturation magnetization increases in a steady manner upon increasing the Nd3+ ion molar ratio from 0.00 up to 0.06, reaching the maximum value of 105.8±0.4 Am2/kg at x = 0.06. It is worth to mention that the result for the saturation magnetization value are higher than that of the bulk material.

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.

Prevalence and screening of active tuberculosis in a prison in the South of Brazil.

SETTING: Tuberculosis (TB) remains a challenge in Brazil, particularly among prison inmates. OBJECTIVE: To assess TB prevalence by active case finding in a public prison in southern Brazil. DESIGN: Prison inmates were screened for TB using the presence of cough and chest X-ray (CXR) from October 2014 to August 2016. Presence of cough, irrespective of duration, and abnormal CXRs were further investigated using laboratory tests. RESULTS: Of 10 326 inmates screened, 196 had confirmed TB (1898/100 000 inmates screened). At the first screening, 1759 inmates presented with cough only, 16 of whom had TB; among those with only abnormal CXR (n = 1273), 92 had TB. Xpert was positive in 155 patients, and negative in 15; these results were confirmed using culture. The remaining 26 patients did not undergo Xpert testing and were confirmed using microscopy (27%), culture (42%) or both (31%). CONCLUSION: The combined use of symptom screening (cough) and CXR was much more effective in maximising TB yield than using either method alone. If patients presenting with cough alone had not been investigated, 10% of TB patients would have been missed; if those with abnormal CXR but no cough had not been investigated, 51% of TB patients would have been missed. We detected high TB prevalence in this prison by using active case finding.

Stabilising lamellar stacks of lipid bilayers with soft confinement and steric effects.

Structure and interactions stabilising the lamellar stack of mixed lipid bilayers in their fluid state are investigated by means of small-angle X-ray scattering. The (electrically neutral) bilayers are composed of a mixtures of lecithin, a zwitterionic phospholipid, and Simulsol, a non-ionic cosurfactant with an ethoxylated polar head. The soft confinement of the bilayer hydrophilic components is varied by changing hydration and bilayer composition, as well as the length of the cosurfactant polar head. Structural transitions are observed at low hydration, in the stacking order for the longer cosurfactant, and in the mixed bilayers for the shorter one. At higher hydration, the swelling of the lamellar stacks occurs with a significant, but continuous evolution in the mixed bilayer structure. The bilayer structural changes are discussed in analogy with the so-called "brush-to-mushroom" transition induced by lateral confinement, relevant for long linear polymers grafted onto rigid surfaces, taking also into account the role of vertical confinement.

Magnetic and structural study of electric double-layered ferrofluid with MnFe(2)O(4)@γ-Fe(2)O(3) nanoparticles of different mean diameters: Determination of the magnetic correlation distance.

Magnetic fluids based on manganese ferrite nanoparticles were studied from the structural point of view through small angle x-rays scattering (SAXS) and from the magnetic point of view through zero-field cooling and field cooling (ZFC-FC) and ac susceptibility measurements (MS). Three different colloids with particles mean diameters of 2.78,3.42, and 6.15 nm were investigated. The size distribution obtained from SAXS measurements follows a log-normal behavior. The ZFC-FC and MS results revealed the presence of an important magnetic interaction between the nanoparticles, characterized by a magnetic correlation distance Λ. The colloidal medium can be pictures as composed by magnetic cluster constituted by N interacting particles. These magnetic clusters are not characterized by a physical aggregation of particles. The energy barrier energy obtained is consistent with the existence of this magnetic clusters. Besides the magnetic interaction between particles, confinement effects must be included to account for the experimental values of the magnetic energy barrier encountered.

Anisotropic Brownian motion in ordered phases of DNA fragments.

Using Fluorescence Recovery After Photobleaching, we investigate the Brownian motion of DNA rod-like fragments in two distinct anisotropic phases with a local nematic symmetry. The height of the measurement volume ensures the averaging of the anisotropy of the in-plane diffusive motion parallel or perpendicular to the local nematic director in aligned domains. Still, as shown in using a model specifically designed to handle such a situation and predicting a non-Gaussian shape for the bleached spot as fluorescence recovery proceeds, the two distinct diffusion coefficients of the DNA particles can be retrieved from data analysis. In the first system investigated (a ternary DNA-lipid lamellar complex), the magnitude and anisotropy of the diffusion coefficient of the DNA fragments confined by the lipid bilayers are obtained for the first time. In the second, binary DNA-solvent system, the magnitude of the diffusion coefficient is found to decrease markedly as DNA concentration is increased from isotropic to cholesteric phase. In addition, the diffusion coefficient anisotropy measured within cholesteric domains in the phase coexistence region increases with concentration, and eventually reaches a high value in the cholesteric phase.

SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the Arg124His mutation.

Human transforming growth factor ß induced protein (TGFBIp) is composed of 683 residues, including an N-terminal cysteine-rich (EMI) domain, four homologous fasciclin domains, and an Arg-Gly-Asp (RGD) motif near the C-terminus. The protein is of interest because mutations in the TGFBI gene encoding TGFBIp lead to corneal dystrophy (CD), a condition where protein aggregates within the cornea compromise transparency. The complete three-dimensional structure of TGFBIp is not yet available, with the exception of a partial X-ray structure of the archetype FAS1 domain derived from Drosophila fasciclin-1. In this study, small-angle X-ray scattering (SAXS) models of intact wild-type (WT) human TGFBIp and a mutant (R124H) are presented. The mutation R124H leads to a variant of granular CD. The deduced structure of the TGFBIp monomer consists of four FAS1 domains in a simple "beads-on-a-string" arrangement, constructed by the superimposition of four consecutive Drosophila fasciclin domains. The SAXS-based model of the TGFBIp R124H mutant displayed no structural differences from WT. Both WT TGFBIp and the R124H mutant formed trimers at higher protein concentrations. The similar association properties and three-dimensional shape of the two proteins suggest that the mutation does not induce any major structural rearrangements, but points towards the role of other corneal-specific factors in the formation of corneal R124H deposits.

Small angle x-ray scattering from lipid-bound myelin basic protein in solution.

The structure of myelin basic protein (MBP), purified from the myelin sheath in both lipid-free (LF-MBP) and lipid-bound (LB-MBP) forms, was investigated in solution by small angle x-ray scattering. The water-soluble LF-MBP, extracted at pH < 3.0 from defatted brain, is the classical preparation of MBP, commonly regarded as an intrinsically unfolded protein. LB-MBP is a lipoprotein-detergent complex extracted from myelin with its native lipidic environment at pH > 7.0. Under all conditions, the scattering from the two protein forms was different, indicating different molecular shapes. For the LB-MBP, well-defined scattering curves were obtained, suggesting that the protein had a unique, compact (but not globular) structure. Furthermore, these data were compatible with earlier results from molecular modeling calculations on the MBP structure which have been refined by us. In contrast, the LF-MBP data were in accordance with the expected open-coil conformation. The results represent the first direct structural information from x-ray scattering measurements on MBP in its native lipidic environment in solution.