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Registros recuperados: 5
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Molecular and morphological characterization of hydrochar produced by microwave-assisted hydrothermal carbonization of cellulose PAB
Guiotoku,Marcela; Hansel,Fabricio Augusto; Novotny,Etelvino Henrique; Maia,Claudia Maria Branco de Freitas.
The objective of this work was to characterize the morphology and molecular composition of the hydrochar produced by microwave-assisted hydrothermal carbonization of cellulose. The produced hydrochar consists mainly of aggregate microspheres with about 2.0 µm in diameter, with aliphatic and aromatic structures and the presence of carbonyl functional groups. The aromatic groups are formed mainly by benzofuran-like structures, being chemically different from common cellulose char. Microwave-assisted hydrothermal carbonization yields a functionalized carbon-rich material similar to that produced by the conventional hydrothermal process.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Anthropogenic dark earth of Amazonia; Biochar; Charcoal; Gas chromatography; Mass spectrometry; Nuclear magnetic resonance.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-204X2012000500008
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Proton NMR characterization of intact primary and metastatic melanoma cells in 2D & 3D cultures Biol. Res.
Ramachandran,Gokula Krishnan; Yeow,Chen Hua.
Abstract Objective To characterize the differences between the primary and metastatic melanoma cell lines grown in 2D cultures and 3D cultures. Methods Primary melanoma cells (WM115) and metastatic melanoma cells (WM266) extracted from a single donor was cultured in 2D as well as 3D cultures. These cells were characterized using proton NMR spectrometry, and the qualitative chemical shifts markers were identified and discussed. Results In monolayer culture (2D), we observed one qualitative chemical shift marker for primary melanoma cells. In spheroid cultures (3D), we observed nine significant chemical shifts, of which eight markers were specific for primary melanoma spheroids, whereas the other one marker was specific to metastatic melanoma...
Tipo: Journal article Palavras-chave: Nuclear magnetic resonance; Proton magnetic resonance spectrometry; Melanoma; Cancer.
Ano: 2017 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602017000100208
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Reproducing the organic matter model of anthropogenic dark earth of Amazonia and testing the ecotoxicity of functionalized charcoal compounds PAB
Linhares,Carolina Rodrigues; Lemke,Jasmin; Auccaise,Ruben; Duó,Daniele Avilez; Ziolli,Roberta Lourenço; Kwapinski,Witold; Novotny,Etelvino Henrique.
The objective of this work was to obtain organic compounds similar to the ones found in the organic matter of anthropogenic dark earth of Amazonia (ADE) using a chemical functionalization procedure on activated charcoal, as well as to determine their ecotoxicity. Based on the study of the organic matter from ADE, an organic model was proposed and an attempt to reproduce it was described. Activated charcoal was oxidized with the use of sodium hypochlorite at different concentrations. Nuclear magnetic resonance was performed to verify if the spectra of the obtained products were similar to the ones of humic acids from ADE. The similarity between spectra indicated that the obtained products were polycondensed aromatic structures with carboxyl groups: a soil...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Daphnia similis; Biochar; Chemical oxidation; Fractionation of humic substances; Nuclear magnetic resonance; Pyrogenic carbon.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-204X2012000500009
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The Ancestral N-Terminal Domain of Big Defensins Drives Bacterially Triggered Assembly into Antimicrobial Nanonets ArchiMer
Loth, Karine; Vergnes, Agnes; Barreto, Cairé; Voisin, Sébastien N; Meudal, Hervé; Da Silva, Jennifer; Bressan, Albert; Belmadi, Nawal; Bachère, Evelyne; Aucagne, Vincent; Cazevielle, Chantal; Marchandin, Hélène; Rosa, Rafael Diego; Bulet, Philippe; Touqui, Lhousseine; Delmas, Agnès F.; Destoumieux-garzón, Delphine.
Big defensins, ancestors of β-defensins, are composed of a β-defensin-like C-terminal domain and a globular hydrophobic ancestral N-terminal domain. This unique structure is found in a limited number of phylogenetically distant species, including mollusks, ancestral chelicerates, and early-branching cephalochordates, mostly living in marine environments. One puzzling evolutionary issue concerns the advantage for these species of having maintained a hydrophobic domain lost during evolution toward β-defensins. Using native ligation chemistry, we produced the oyster Crassostrea gigas BigDef1 (Cg-BigDef1) and its separate domains. Cg-BigDef1 showed salt-stable and broad-range bactericidal activity, including against multidrug-resistant human clinical isolates...
Tipo: Text Palavras-chave: MRSA; Antimicrobial peptides; Antimicrobial resistance; Defensins; Fibrils; Innate immunity; Mechanisms of action; Nuclear magnetic resonance.
Ano: 2019 URL: https://archimer.ifremer.fr/doc/00588/70057/68000.pdf
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The structural molecular biology network of the State of São Paulo, Brazil Anais da ABC (AABC)
Barbosa,João A.R.G.; Netto,Luis E.S.; Farah,Chuck S.; Schenkman,Sergio; Meneghini,Rogério.
This article describes the achievements of the Structural Molecular Biology Network (SMolBNet), a collaborative program of structural molecular biology, centered in the State of São Paulo, Brazil, and supported by São Paulo State Funding Agency (FAPESP). It gathers twenty scientific groups and is coordinated by the scientific staff of the Center of Structural Molecular Biology, at the National Laboratory of Synchrotron Light (LNLS), in Campinas. The SMolBNet program has been aimed at 1) solving the structure of proteins of interest related to the research projects of the groups. In some cases, the choice has been to select proteins of unknown function or of possible novel structure obtained from the sequenced genomes of the FAPESP genomic program; 2)...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Structural genomics; Protein crystallography; Nuclear magnetic resonance; Protein structure.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652006000200006
Registros recuperados: 5
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