5 resultados para ACID AMIDE HYDROLASE

em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"


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A critical revision of literature as regards to the drug stability in the presence of surfactants were realized. The functional groups envolved in the drug decomposition were used to the development of the discussion. The analysis indicated that the detergent effect can be used to control the rates and mechanisms of drug decomposition and to obtain specific information about the drug reactivity in the environment of pharmacological action.

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In this work, we investigate Langmuir monolayers froth an amide extracted from dried roots of Ottonia propinqua, a native Brazilian plant believed to exhibit anesthetic and hallucinogen activities. In addition to producing monolayers from the amide itself, we probe the molecular-level action of the amide on phospholipids employed as simple membrane models. The surface pressure-molecular area (pi-A) isotherms for the amide were little affected by a number of subphase conditions. Almost no changes were observed upon varying the compression speed, spreading volume onto the surface, ions in the subphase, ionic strength and the solution solvent. However, stronger effects occurred when the subphase temperature and pH were altered, as the isotherms were shifted to larger areas with increasing temperatures and decreasing pHs. These results are discussed in terms of the molecular packing adopted by the amide at the air-water interface. In the mixed films with arachidic acid, the area per molecule varied linearly with the concentration of amide, probably due to phase separation. on the other hand, in the mixed films with dipalmitoyl phosphatidyl choline (DPPC), small amounts of the amide were sufficient to change the pi-A isotherms significantly. This points to a strong molecular-level interaction, probably between the phosphate group in the zwitterion of DPPC and the nitrogen from the amidic group. (c) 2004 Elsevier B.V. All rights reserved.

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This study determined if dentin proteases are denatured by phosphoric acid (PA) used in etch-and-rinse dentin adhesives. Dentin beams were completely demineralized with EDTA for 30 days. We acid-etched experimental groups by exposing the demineralized dentin beams to 1, 10, or 37 mass% PA for 15 sec or 15 min. Control beams were not exposed to PA but were incubated in simulated body fluid for 3 days to assay their total endogenous telopeptidase activity, by their ability to solubilize C-terminal crosslinked telopeptides ICTP and CTX from insoluble dentin collagen. Control beams released 6.1 ± 0.8 ng ICTP and 0.6 ± 0.1 ng CTX/mg dry-wt/3 days. Positive control beams pre-incubated in p-aminophenylmercuric acetate, a compound known to activate proMMPs, released about the same amount of ICTP peptides, but released significantly less CTX. Beams immersed in 1, 10, or 37 mass% PA for 15 sec or 15 min released amounts of ICTP and CTX similar to that released by the controls (p > 0.05). Beams incubated in galardin, an MMP inhibitor, or E-64, a cathepsin inhibitor, blocked most of the release of ICTP and CTX, respectively. It is concluded that PA does not denature endogenous MMP and cathepsin activities of dentin matrices. © 2013 International & American Associations for Dental Research.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)