982 resultados para CYSTEINE PROTEASE INHIBITORS
Resumo:
Inibidores de corrosão são substâncias que quando adicionadas a um meio agressivo, diminuem ou previnem a reação de oxidação de um metal com este meio e/ou as reações de redução de espécies presentes no meio. Para a inibição da corrosão de cobre e suas ligas em meios ácidos ou neutros, o inibidor mais empregado é o benzotriazol (BTAH), o qual forma complexos com os íons Cu (I) e Cu (II) na superfície do metal, diminuindo o processo corrosivo. A preocupação com a preservação ambiental e a toxicidade de inibidores de corrosão vem sendo discutida na literatura. Vários estudos têm-se intensificado usando aminoácidos, como proposta para substituição ao BTAH, considerado tóxico. Entre os aminoácidos estudados, dois apresentavam enxofre em suas moléculas (cisteína e metionina) e um outro sem heteroátomo na cadeira lateral (glicina). As concentrações variaram entre 10-2 a 10-4 mol/L e pH da solução entre 7,2 e 8,4. Foram realizadas medidas gravimétricas (ensaios de imersão total) e técnicas eletroquímicas, tais como polarização potenciodinâmica e espectroscopia de impedância eletroquímica. A caracterização morfológica da superfície do substrato após os ensaios de imersão total (743 horas) foi feita por meio de microscopia eletrônica de varredura (MEV), espectroscopia de raios X por dispersão de energia (EDS ou EDX) e difração de raios X (DRX). Embora os resultados com aminoácidos tenham sido sempre muito inferiores àqueles obtidos na presença de BTAH, comportamentos semelhantes em função da concentração dos aminoácidos puderam ser observados pelos diagramas de Nyquist. Contudo, com exceção dos resultados verificados para o meio contendo cisteína 10-2 mol/L, todas as eficiências de inibição para os meios contendo aminoácidos, obtidas pelos ensaios de imersão total, foram negativas, mostrando que o tempo de exposição também pode ser relevante para o desempenho destes inibidores. Entre todos os aminoácidos testados, os meios contendo glicina apresentaram os piores desempenhos anticorrosivos, inclusive acelerando o processo de dissolução anódica do cobre. Esse resultado pode estar relacionado à faixa de pH das soluções testadas e à solubilidade dos complexos de cobre formados com os aminoácidos, mostrando que uma faixa ótima de pH também deve ser assegurada para aprimorar a ação destes aminoácidos como inibidores de corrosão
Resumo:
Technology roadmapping workshops are essentially a social mechanism for exploring, creating, shaping and implementing ideas. The front-end of a roadmapping session is based on brainstorming in order to tap into the group's diverse knowledge. The aim of this idea stimulation activity is to capture and share as many perspectives as possible across the full scope of the area of interest. The premise to such group brainstorming is that the sharing and exchange of ideas leads to cognitive stimulation resulting in a greater overall group idea generation performance in terms of the number, variety and originality of ideas. However, it must be recognized that the ideation stage in a roadmapping workshop is a complex psychosocial phenomenon with underlying cognitive and social processes. Thus, there are downsides to group interactions and these must be addressed in order to fully benefit from the power of a roadmapping workshop. This paper will highlight and discuss the key cognitive and social inhibitors involved. These include: production blocking, evaluation apprehension, free riding/social loafing, low norm setting/matching. Facilitation actions and process adjustments to counter such negative factors will be identified so as to provide a psychosocial basis for improving the running of roadmapping workshops. © 2009 PICMET.
Resumo:
Wasp is an important venomous animal that can induce human fatalities. Coagulopathy is a clinical symptom after massive wasp stings, but the reason leading to the envenomation manifestation is still not known. In this paper, a toxin protein is purified and characterized by Sephadex G-75 gel filtration, CM-Sephadex C-25 cationic exchange and fast protein liquid chromatography (FPLC) from the venom of the wasp, Vespa magnifica (Smith). This protein, named magnvesin. contains serine protease-like activity and inhibits blood coagulation. The cDNA encoding magnvesin is cloned from the venom sac cDNA library of the wasp. The deduced protein from the cDNA is composed of 305 amino acid residues. Magnvesin shares 52% identity with allergen serine protease from the wasp Polistes dominulus. Magnvesin exerted its anti-coagulant function by hydrolyzing coagulant factors TF, VII, VIII, IX and X. (c) 2008 Elsevier Ltd. All rights reserved.
Resumo:
Horseflies are economically important blood-feeding arthropods and also a nuisance for humans and vectors for filariasis. They rely heavily on the pharmacological properties of their saliva to get a blood meal and suppress immune reactions of hosts. Little information is available on antihemostatic substances in horsefly salivary glands; especially no horsefly immune suppressants have been reported. By proteomics or peptidomics and coupling transcriptome analysis with pharmacological testing, several families of proteins or peptides, which act mainly on the hemostatic system or immune system of the host, were identified and characterized from 30,000 pairs salivary glands of the horsefly Tabanus yao (Diptera, Tabanidae). They are: (i) a novel family of inhibitors of platelet aggregation including two members, which possibly inhibit platelet aggregation by a novel mechanism and act on platelet membrane, (ii) a novel family of immunosuppressant peptides including 12 members, which can inhibit interferon-gamma production and increase interleukin-10 secretion, (iii) a serine protease inhibitor with 56 amino acid residues containing anticoagulant activity, (iv) a serine protease with anticoagulant activity, (v) a protease with fibrinogenolytic activity, (vi) three families of antimicrobial peptides including six members, (vii) a hyaluronidase, (viii) a vasodilator peptide, which is an isoform of vasotab identified from Hybomitra bimaculata, and interestingly (ix) two metallothioneins, which are the first metallothioneins reported from invertebrate salivary glands. The current work will facilitate the understanding of the molecular mechanisms of the ectoparasite-host relationship and help in identifying novel vaccine targets and novel leading pharmacological compounds.
Resumo:
The Ag5 proteins are the most abundant and immunogenic proteins in the venom secretory ducts of stinging insects. An antigen 5-like protein (named tabRTS) composed of 221 amino acid residues was purified and characterized from the salivary glands of the horsefly, Tabanus yao (Diptera, Tabanidae). Its cDNA was cloned from the cDNA library of the horsefly's salivary gland. TabRTS containing the SCP domain (Sc7 family of extracellular protein domain) was found in insect antigen 5 proteins. More interestingly, there is an Arg-Thr-Ser (RTS) disintegrin motif at the C-terminus of tabRTS. The RTS motif is positioned in a loop bracketed by cysteine residues as those found in RTS-disintegrins of Crotalidae and Viperidae snake venoms, which act as angiogenesis inhibitors. Endothelial Cell Tube formation assay in vitro and chicken chorioallantoic membrane (CAM) angiogenesis assay in vivo were performed as to investigate the effect of tabRTS on angiogenesis. It was found that tabRTS could significantly inhibit angiogenesis in vitro and in vivo. Anti-alpha(1)beta(1) monoclonal antibody could dose-dependently inhibit the anti-angiogenic activity of tabRTS. This result indicated that tabRTS possibly targets the alpha(1)beta(1) integrin to exert the anti-angiogenic activity as snake venom RTS-/KTS-disintegrins do. The current work revealed the first angiogenesis inhibitor protein containing RTS motif from invertebrates, a possible novel type of RTS-disintegrin. (C) 2009 Elsevier Ltd. All rights reserved.
Resumo:
A number of inactive serine protease homologues (SPHs), which have poorly understood functions, have been identified in invertebrates and vertebrates. Recently, several SPH transcripts have been reported from snake venom glands, which provide potential ne
Resumo:
A fibrin(ogen)olytic serine protease from Trimeresurus jerdonii venom was identified and purified to SDS-polyacrylamide gel electrophoresis homogeneity. It is a single chain polypeptide with a molecular weight of 32 kDa under reduced condition and 28 kDa
Resumo:
Three 26 kDa proteins, named as TJ-CRVP, NA-CRVP1 and NA-CRVP2, were isolated from the venoms of Trimeresurus jerdonii and Naja atra, respectively. The N-terminal sequences of TJ-CRVP and NA-CRVPs were determined. These components were devoid of the enzymatic activities tested, such as phospholipase A(2), arginine esterase, proteolysis, L-amino acid oxidase, 5' nucleotidase, acetylcholinesterase. Furthermore, these three components did not have the following biological activities: coagulant and anticoagulant activities, lethal activity, myotoxicity, hemorrhagic activity, platelet aggregation and platelet aggregation-inhibiting activities. These proteins are named as cysteine-rich venom protein (CRVP) because their sequences showed high level of similarity with mammalian cysteine-rich secretory protein (CRISP) family. Recently, some CRISP-like proteins were also isolated from several different snake venoms, including Agkistrodon blomhoffi, Trimeresurus flavoviridis, Lanticauda semifascita and king cobra. We presumed that CRVP might be a common component in snake venoms. Of particular interest, phylogenetic analysis and sequence alignment showed that NA-CRVP1 and ophanin, both from elapid snakes, share higher similarity with CRVPs from Viperidae snakes. (C) 2003 Elsevier Ltd. All rights reserved.
Resumo:
A novel kinin-releasing and fibrin (ogen)olytic enzyme termed jerdonase was purified to homogeneity from the venom of Trimeresurus jerdonii by DEAE Sephadex A-50 anion exchange, Sephadex G-100 (superfine) gel filtration and reverse-phase high performance liquid chromatography (RP-HPLC). Jerdonase migrated as a single band with an approximate molecular weight of 55 kD under the reduced conditions and 53 kD under the non-reduced conditions. The enzyme was a glycoprotein containing 35.8% neutral carbohydrate. The N-terminal amino acid sequence of jerdonase was determined to be IIGGDECNINEHPFLVALYDA, which showed high sequence identity to other snake venom serine proteases. Jerdonase catalyzed the hydrolysis of BAEE, S-2238 and S-2302, which was inhibited by phenymethylsulfonyl fluoride (PMSF), but not affected by ethylenediaminetetraacetic acid (EDTA). Jerdonase preferentially cleaved the Aalpha-chain of human fibrinogen with lower activity towards Bbeta-chain. Moreover, the enzyme hydrolyzed bovine low-molecular-mass kininogen and releasing bradykinin. In conclusion, all results indicated that jerdonase was a multifunctional venom serine protease.
Resumo:
The trypsin-like serine protease (Tryp_SPc) family is ubiquitous in animals and plays diverse roles, especially in the digestive system, in different phyla. In the mosquito, some Tryp_SPc proteases make important contributions to the digestion of the bloo
Resumo:
A variety of N-acetyl-o-aryl-1,2-didehydroethylamines were synthesized by direct reduction-acetylation of beta-aryl-nitroolefins and assayed as HIV-1 non-nucleoside reverse transcriptase inhibitors (NNRTIs) for the first time. Compound 7a exhibited a TI v
Resumo:
Three new types of aryl diketo acid (ADK) isosteres were designed by conversion of the biologically labile 1,3-diketo unit into heteroaromatic motif such as isoxazole, isothiazole, or 1H-pyrazole to improve the physicochemical property of ADK-based HIV-1