5,667 research outputs found

    The Nylon Scintillator Containment Vessels for the Borexino Solar Neutrino Experiment

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    Borexino is a solar neutrino experiment designed to observe the 0.86 MeV Be-7 neutrinos emitted in the pp cycle of the sun. Neutrinos will be detected by their elastic scattering on electrons in 100 tons of liquid scintillator. The neutrino event rate in the scintillator is expected to be low (~0.35 events per day per ton), and the signals will be at energies below 1.5 MeV, where background from natural radioactivity is prominent. Scintillation light produced by the recoil electrons is observed by an array of 2240 photomultiplier tubes. Because of the intrinsic radioactive contaminants in these PMTs, the liquid scintillator is shielded from them by a thick barrier of buffer fluid. A spherical vessel made of thin nylon film contains the scintillator, separating it from the surrounding buffer. The buffer region itself is divided into two concentric shells by a second nylon vessel in order to prevent inward diffusion of radon atoms. The radioactive background requirements for Borexino are challenging to meet, especially for the scintillator and these nylon vessels. Besides meeting requirements for low radioactivity, the nylon vessels must also satisfy requirements for mechanical, optical, and chemical properties. The present paper describes the research and development, construction, and installation of the nylon vessels for the Borexino experiment

    Fmoc–RGDS based fibrils: atomistic details of their hierarchical assembly

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    We describe the 3D supramolecular structure of Fmoc–RGDS fibrils, where Fmoc and RGDS refer to the hydrophobic N-(fluorenyl-9-methoxycarbonyl) group and the hydrophilic Arg-Gly-Asp-Ser peptide sequence, respectively. For this purpose, we performed atomistic all-atom molecular dynamics simulations of a wide variety of packing modes derived from both parallel and antiparallel ß-sheet configurations. The proposed model, which closely resembles the cross-ß core structure of amyloids, is stabilized by p–p stacking interactions between hydrophobic Fmoc groups. More specifically, in this organization, the Fmoc-groups of ß-strands belonging to the same ß-sheet form columns of p-stacked aromatic rings arranged in a parallel fashion. Eight of such columns pack laterally forming a compact and dense hydrophobic core, in which two central columns are surrounded by three adjacent columns on each side. In addition to such Fmoc¿Fmoc interactions, the hierarchical assembly of the constituent ß-strands involves a rich variety of intra- and inter-strand interactions. Accordingly, hydrogen bonding, salt bridges and p–p stacking interactions coexist in the highly ordered packing network proposed for the Fmoc–RGDS amphiphile. Quantum mechanical calculations, which have been performed to quantify the above referred interactions, confirm the decisive role played by the p–p stacking interactions between the rings of the Fmoc groups, even though both inter-strand and intra-strand hydrogen bonds and salt bridges also play a non-negligible role. Overall, these results provide a solid reference to complement the available experimental data, which are not precise enough to determine the fibril structure, and reconcile previous independent observations.Peer ReviewedPostprint (published version

    Effect of Solvent Choice on the Self-Assembly Properties of a Diphenylalanine Amphiphile Stabilized by an Ion Pair

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    A diphenylalanine (FF) amphiphile blocked at the C terminus with a benzyl ester (OBzl) and stabilized at the N terminus with a trifluoroacetate (TFA) anion was synthetized and characterized. Aggregation of peptide molecules was studied by considering a peptide solution in an organic solvent and adding pure water, a KCl solution, or another organic solvent as co-solvent. The choice of the organic solvent and co-solvent and the solvent/ co-solvent ratio allowed the mixture to be tuned by modulating the polarity, the ionic strength, and the peptide concentration. Differences in the properties of the media used to dissolve the peptides resulted in the formation of different self-assembled microstructures (e.g. fibers, branched-like structures, plates, and spherulites). Furthermore, crystals of TFA·FFOBzl were obtained from the aqueous peptide solutions for Xray diffraction analysis. The results revealed a hydrophilic core constituted by carboxylate (from TFA), ester, and amide groups, and the core was found to be surrounded by a hydrophobic crown with ten aromatic rings. This segregated organization explains the assemblies observed in the different solvent mixtures as a function of the environmental polarity, ionic strength, and peptid

    Effect of Solvent Choice on the Self-Assembly Properties of a Diphenylalanine Amphiphile Stabilized by an Ion Pair

    Get PDF
    A diphenylalanine (FF) amphiphile blocked at the C terminus with a benzyl ester (OBzl) and stabilized at the N terminus with a trifluoroacetate (TFA) anion was synthetized and characterized. Aggregation of peptide molecules was studied by considering a peptide solution in an organic solvent and adding pure water, a KCl solution, or another organic solvent as co-solvent. The choice of the organic solvent and co-solvent and the solvent/co-solvent ratio allowed the mixture to be tuned by modulating the polarity, the ionic strength, and the peptide concentration. Differences in the properties of the media used to dissolve the peptides resulted in the formation of different self-assembled microstructures (e.g. fibers, branched-like structures, plates, and spherulites). Furthermore, crystals of TFAFF-OBzl were obtained from the aqueous peptide solutions for X-ray diffraction analysis. The results revealed a hydrophilic core constituted by carboxylate (from TFA), ester, and amide groups, and the core was found to be surrounded by a hydrophobic crown with ten aromatic rings. This segregated organization explains the assemblies observed in the different solvent mixtures as a function of the environmental polarity, ionic strength, and peptide concentration

    Interface Property of Collagen and Hydroxyapatite in Bone

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    When looking at bone at the nanoscale, it consists of a matrix of type I collagen and hydroxyapatite (HAP). Type I collagen is the most abundant protein in the body and together with the mineral HAP [Ca10(PO4)6(OH)2] is responsible for most of the structural integrity of bone. Collagen fibrils in bone contain HAP platelets of varying size dispersed between the collagen. The composition of the type I collagen is predicted to play a role in the mechanical properties of the interface. Our research looks at healthy heterotrimeric collagen and mutated homotrimeric collagen containing three identical chains. Both types of collagen are tested using Steered Molecular Dynamics (SMD) [1] in shearing and peeling directions along the hydroxyl (OH) surface of HAP. The Bell model is also applied to analyze the energy associated with rupturing collagen in shear. The results show that the force required to separate collagen from HAP is not affected by mutation, but the structure of the collagen considerably changes the distribution of hydrogen bonds between collagen-collagen and collagen-HAP interfaces. In shear, homotrimeric collagen forms between 20-40% fewer hydrogen bonds than heterotrimeric collagen. In both shearing and peeling, the number of collagen-water hydrogen bonds increases by roughly 100% before rupture. This research has led to the development of an HAP inspired structure. Currently 3D printed using ABS plastic

    Resource Letter NO-1: Nonlinear Optics

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    This Resource Letter provides a guide to the literature on nonlinear optics. Books, journals, and websites are introduced that cover the general subject. Journal articles and websites are cited covering the following topics: second-order nonlinearities in transparent media including second-harmonic generation and optical parametric oscillation, third-order and higher nonlinearities, nonlinear refractive index, absorptive nonlinearities such as saturable absorption and multiphoton absorption, and scattering nonlinearities such as stimulated Raman scattering and stimulated Brillouin scattering. Steady-state and transient phenomena, fiber optics, solitons, nonlinear wave mixing, optical phase conjugation, nonlinear spectroscopy, and multiphoton microscopy are all outlined

    Wettability of nonwoven polymeric nanofiber mats

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    The wettability of heterogeneous materials has been attracting special interest by academia and industrial sector given the need to development self-cleaning Nonwoven nanofiber mats have demonstrated potential given its hydrophobicity granted by the ultimate structure of the system, small fiber diameter and small pores giving rise to effects such as the Cassie-Baxter. This thesis analyzed the wettability of a wide range of polymeric systems. Nanofiber mats were manufactured using the Forcespinning® technology. Samples were prepared at different polymeric concentrations and rotational speeds to alter fiber size; density of the mat was also altered to evaluate the effect of porosity on the wettability. Scanning Electron Microscopy (SEM) was used to characterize the mats and contact angle studies were conducted to better understand wettability of the developed surfaces

    Interface Property of Collagen and Hydroxyapatite in Bone and Developing Bioinspired Materials

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    Bone at the nanoscale consists of type I collagen and hydroxyapatite (HAP). Type I collagen and HAP [Ca10(PO4)6(OH)2] are responsible for most of the structural integrity of bone. Collagen fibrils contain HAP platelets of varying size dispersed between the collagen. We investigate heterotrimeric collagen interaction with HAP using Steering Molecular Dynamics to obtain the force-displacement relation as the collagen is undergoing shearing and peeling on the surface of HAP. Results indicate that the collagen requires 40% less force to separate form the HAP surface under peeling, when compared to shear loading conditions. In both shearing and peeling, the number of collagen-water hydrogen bonds increases by approximately 100% before rupture. We developed an HAP inspired structure and 3D printed it using ABS plastic. This bio-inspired material could have several potential applications in engineering and medicine
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