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The role from the physician for patients with lung cancer. The updating report.
Leptin is a hormone that has a fundamental role in the regulation of feeding and energy balance. A developed specific SPRi immunosensor for leptin may be a new tool for leptin determination in blood plasma. The immunosensor consists of rabbit anti-leptin antibody immobilized on a gold chip via cysteamine linker, using the EDC/NHS protocol. Non-fluidic array SPRi is used for analytical signal formation. Under optimized conditions, the linear response range of the immunosensor covers concentrations from 0.23 to 5 ng mL-1. The LOD of the immunosensor is 0.07 ng mL-1, and the LOQ is 0.23 ng mL-1. The precision of measurement depends on leptin concentration, and is between 9.1% and 2.2%. Recoveries of the leptin spike are between 97% and 110%. The immunosensor and related analytical method were validated by parallel determination of leptin in series of plasma from children suffering from malnutrition and a control group, using Enzyme-Linked Immunosorbent Assay (ELISA) and SPRi. Pearson's correlation coefficient was equal to 0.991. The developed immunosensor and related method are more direct, faster and much simpler than ELISA.We report an alternating-reduction approach by galvanic replacement and co-reduction to enable incorporation of Pd into Pt shell, and the obtained PtPd hollow nanocubes with an enhanced alloy effect and highly active 100 facets show high catalytic activity and superior durability in the methanol oxidation reaction.Injectable hydrogels are attractive for therapeutic delivery because they can be locally administered through minimally-invasive routes. Charge-complementary peptide nanofibers provide hydrogels that are suitable for encapsulation of biotherapeutics, such as cells and proteins, because they assemble under physiological temperature, pH, and ionic strength. However, relationships between the sequences of charge-complementary peptides and the physical properties of the hydrogels that they form are not well understood. Here we show that hydrogel viscoelasticity, pore size, and pore structure depend on the pairing of charge-complementary "CATCH(+/-)" peptides. Oscillatory rheology demonstrated that co-assemblies of CATCH(4+/4-), CATCH(4+/6-), CATCH(6+/4-), and CATCH(6+/6-) formed viscoelastic gels that can recover after high-shear and high-strain disruption, although the extent of recovery depends on the peptide pairing. Cryogenic scanning electron microscopy demonstrated that hydrogel pore size and pore wall also depend on peptide pairing, and that these properties change to different extents after injection. In contrast, no obvious correlation was observed between nanofiber charge state, measured with ζ-potential, and hydrogel physical properties. CATCH(4+/6-) hydrogels injected into the subcutaneous space elicited weak, transient inflammation whereas CATCH(6+/4-) hydrogels induced stronger inflammation. MPTP No antibodies were raised against the CATCH(4+) or CATCH(6-) peptides following multiple challenges in vehicle or when co-administered with an adjuvant. These results demonstrate that CATCH(+/-) peptides form biocompatible injectable hydrogels with viscoelastic properties that can be tuned by varying peptide sequence, establishing their potential as carriers for localized delivery of therapeutic cargoes.A novel and versatile toolkit approach for the functionalization of biomaterials of different nature is described. This methodology is based on the solid-phase conjugation of specific anchoring units onto a resin-bound azido-functionalized peptide by using click chemistry. A synergistic multifunctional peptidic scaffold with cell adhesive properties was used as a model compound to showcase the versatility of this new approach. Titanium, gold and polylactic acid surfaces were biofunctionalized by this method, as validated by physicochemical surface characterization with XPS. In vitro assays using mesenchymal stem cells showed enhanced cell adhesion on the functionalized samples, proving the capacity of this strategy to efficiently bioactivate different types of biomaterials.Mechanochemistry refers to unusual chemical reactions induced by mechanical energy at room temperatures. It has attracted increased attention because of advantages, such as being a solution-free, energy saving, high-productivity and low-temperature process. However, there is limited understanding of the mechanochemical process because mechanochemistry is often conducted using closed milling devices, which are often regarded as a black box. This feature article shows that mechanochemical reactions can be controlled by varying milling parameters, such as the mechanical force, milling intensity, time and atmosphere. New nanomaterials with doped and functionalized structures can be produced under controlled conditions, which provide a critical insight for understanding mechanochemistry. A fundamental mechanism investigation using force microscopy is discussed.A small percentage of an impurity was shown, via scanning tunneling microscopy, to drastically change the on-surface self-assembly behavior of an aromatic tetracarboxylic acid, by initiating the nucleation and growth of a different polymorph. Molecular modelling simulations were used to shed further light onto the dopant-controlled assembly behaviour.The coalescence of two Fe8N as well as the structure of the Fe16N2 cluster were studied using density functional theory with the generalized gradient approximation and a basis set of triple-zeta quality. It was found that the coalescence may proceed without an energy barrier and that the geometrical structures of the resulting clusters depend strongly on the mutual orientations of the initial moieties. The dissociation of N2 is energetically favorable on Fe16, and the nitrogen atoms share the same Fe atom in the lowest energy state of the Fe16N2 species. The attachment of two nitrogen atoms leads to a decrease in the total spin magnetic moment of the ground-state Fe16 host by 6 μB due to the peculiarities of chemical bonding in the magnetic clusters. In order to gain insight into the dependence of properties on charge and to estimate the bonding energies of both N atoms, we performed optimizations of Fe16N and the singly charged ions of both Fe16N2 and Fe16N. It was found that the electronic properties of the Fe16N2 cluster, such as electron affinity and ionization energy, do not appreciably depend on the attachment of nitrogen atoms but that the average binding energy per atom changes significantly.
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