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A sensitive bioassay for destruxins, cyclodepsipeptides from the culture filtrates of the entomopathogenic fungus Metarhizium anisopliae (Metsch.) Sorok. Anais da SEB
Samuels,Richard I..
Destruxin A, a toxic cyclodepsipeptide, was purified from culture filtrates of the entomopathogenic fungus Metarhizium anisopliae (Metsch.) Sorok. by Reverse-Phase HPLC, and assayed for its effects on a larval Manduca sexta (L.) (Lepidoptera: Sphingidae) heart preparation. Destruxin A was found to cause reversible and dose-dependent acceleration of the heart beat. The heart bioassay was highly sensitive to pulse applications of destruxin A at concentrations as low as 35 pmol. Because of its high level of sensitivity, the M. sexta heart bioassay could be used to detect and quantify destruxins in tissue extracts from mycosed insects or to confirm bioactivity of HPLC fractions. The site of action of Destruxin A was not determined. However, this toxin did not...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Insecta; Manduca sexta; Heart; Toxin; Peptide; Destruxin.
Ano: 1998 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0301-80591998000200009
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Activity of the antimicrobial peptide P34 against bovine alphaherpesvirus type 1 Ciência Rural
Castro,Clarissa Caetano de; Silva,Débora Scopel e; Costa,Géssica Aracéli; Fischer,Geferson; Vargas,Gilberto D’Avila; Brandelli,Adriano; Lima,Marcelo de; Motta,Amanda de Souza da; Hübner,Silvia de Oliveira.
ABSTRACT: Previous studies have demonstrated the antimicrobial activity of the peptide P34. In this study, the antiviral potential of P34 and the in vitro mechanism of action were investigated against bovine alphaherpesvirus type 1 (BoHV1). P34 exhibited low toxicity, a high selectivity index (22.9) and a percentage of inhibition of up to 100% in MDBK cells. Results from antiviral assays indicated that P34 did not interact with cell receptors, but it was able to inhibit the viral penetration immediately after pre-adsorption. In addition, BoHV1 growth curve in MDBK cells in the presence of P34 revealed a significant reduction in virus titer only 8h post-infection, also suggesting an important role at late stages of the replicative cycle. Virucidal effect...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antiviral; Herpesvirus; Peptide.
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-84782017000600451
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Anti-parasitic peptides from arthropods and their application in drug therapy. Repositório Alice
LACERDA, A. F.; PELEGRINI, P. B.; OLIVEIRA, D. M. de; VASCONCELOS, E. A. R.; GROSSI-DE-SA, M. F..
2016
Tipo: Artigo em periódico indexado (ALICE) Palavras-chave: Anti-parasitic; Hostinsects; Tropical diseases; Protein; Peptide.
Ano: 2016 URL: http://www.alice.cnptia.embrapa.br/handle/doc/1056203
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Bradykinin, insulin, and glycemia responses to exercise performed above and below lactate threshold in individuals with type 2 diabetes BJMBR
Asano,R.Y.; Browne,R.A.V.; Sales,M.M.; Arsa,G.; Moraes,J.F.V.N.; Coelho-Júnior,H.J.; Moraes,M.R.; Oliveira-Silva,I.; Atlas,S.E.; Lewis,J.E.; Simões,H.G..
The aim of this study was to analyze the acute responses of bradykinin, insulin, and glycemia to exercise performed above and below lactate threshold (LT) in individuals with type 2 diabetes mellitus (T2D). Eleven participants with a diagnosis of T2D randomly underwent three experimental sessions 72 h apart: 1) 20 min of exercise performed at 120% of LT (120%LT), 2) 20 min of exercise performed at 80% of LT (80%LT), and 3) 20 min of control session. Blood glucose was analyzed before, during, and at 45 min post-exercise. Bradykinin and insulin were analyzed before and at 45 min post-exercise. Both exercise sessions elicited a parallel decrease in glucose level during exercise (P≤0.002), with a greater decrease being observed for 120%LT (P=0.005). Glucose...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Metabolic disease; Aerobic exercise; Peptide; Insulin resistance.
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2017001100607
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Caractérisation et analyse de l'expression des pénaeidines, peptides antimicrobiens isolés chez la crevette pénéide Penaeus vannamei (Crustacea, Decapoda) ArchiMer
Destoumieux, Delphine.
Haemocytes are the key elements of a complex defence system on which crustacean immunity is largely based. We report here for the first time in a crustacean that haemocytes are involved in the synthesis of antimicrobial peptides similar to those described in other arthropod classes. These molecules isolated from the penaeid shrimp Penaeus vannamei are members of an homogeneous farnily which differ from the antimicrobial peptides previously described in that they combine in a single molecule a proline-rich arninoterminal domain, and a cyclic carboxy-terminal domain containing three intramolecular disulphide bridges. In addition, penaeidins bear post-translational modifications at their arnino- and carboxy-termini. Five molecules of the penaeidin family were...
Tipo: Text Palavras-chave: Crustacé; Crevette; Immunité; Hémocyte; Peptide; Antimicrobien; Cationique.
Ano: 1998 URL: http://archimer.ifremer.fr/doc/00440/55111/56564.pdf
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Characterization of Leiurus abdullahbayrami (Scorpiones: Buthidae) venom: peptide profile, cytotoxicity and antimicrobial activity J. Venom. Anim. Toxins incl. Trop. Dis.
Erdeş,Efe; Doğan,Tuğba Somay; Coşar,İlhan; Danışman,Tarık; Kunt,Kadir Boğaç; Şeker,Tamay; Yücel,Meral; Özen,Can.
Background Scorpion venoms are rich bioactive peptide libraries that offer promising molecules that may lead to the discovery and development of new drugs.Leiurus abdullahbayrami produces one of the most potent venoms among Turkish scorpions that provokes severe symptoms in envenomated victims.Methods In the present study, the peptide profile of the venom was investigated by electrophoretic methods, size-exclusion and reversed-phase chromatography and mass spectroscopy. Cytotoxic and antimicrobial effects were evaluated on a breast cancer cell line (MCF-7) and various bacterial and fungal species.Results Proteins make up approximately half of the dry weight of L. abdullahbayrami crude venom. Microfluidic capillary electrophoresis indicated the presence of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Scorpion venom; Toxin; Peptide; Leiurus abdullahbayrami; Microfluidic capillary; Electrophoresis; Peptidomics; Venomics; Cytotoxicity; Antimicrobial activity; Turkey.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200338
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Clavanin bacterial sepsis control using a novel methacrylate nanocarrier. Repositório Alice
SAÚDE, A. C. M.; OMBREDANE, A. S.; SILVA, O. N.; BARBOSA, J. A. R. G.; MORENO, S. E.; ARAUJO, A. C. G.; FALCAO, R.; SILVA, L. P.; DIAS, S. C.; FRANCO, O. L..
2014
Tipo: Artigo em periódico indexado (ALICE) Palavras-chave: Antimicrobial; Nanoparticles; Nanobiotechnology; Peptide.
Ano: 2014 URL: http://www.alice.cnptia.embrapa.br/handle/doc/1005987
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Intein-mediated expression of cecropin in Escherichia coli Electron. J. Biotechnol.
Díaz,Mauricio; Venturini,Elena; Marchetti,Stefano; Arenas,Gloria; Marshall,Sergio H.
Different strategies have been used to overcome the difficulties to produce antimicrobial peptides. Here we used Intein Mediated Purification with an Affinity Chitin-binding Tag (IMPACT-System, New England Biolabs) for the expression of the antimicrobial peptide cecropin to reduce its sensitivity to intracellular proteases and use its inducible self-cleaving capability to remove the carrier. Cecropin was cloned into suitable expression vector pTYB11, and expression induced by IPTG in Escherichia coli ER2566. The use of 22ºC induction allowed the expression of cecropin with its intein carrier in soluble form. Cell extracts were purified by chitin affinity chromatography and intein-mediated splicing of the target protein was achieved by thiol addition,...
Tipo: Journal article Palavras-chave: Antimicrobial; Cecropin; Fusion; Intein; Peptide; Soluble.
Ano: 2012 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582012000200003
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Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros J. Venom. Anim. Toxins incl. Trop. Dis.
Fucase,Tamara M.; Sciani,Juliana M.; Cavalcante,Ingrid; Viala,Vincent L.; Chagas,Bruno B.; Pimenta,Daniel C.; Spencer,Patrick J..
Abstract Background: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13 residues with a high number of proline residues and the tripeptide Ile-Pro-Pro (IPP-tripeptide) in the C-terminus region and have a conserved N-terminal pyroglutamate residue. As a whole, the action of the BPPs on prey and snakebite victims results in the decrease of the blood pressure. The aim of this work was to isolate and characterize novel BPPs from the venom of Bitis gabonica rhinoceros....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Peptide; Hypotension; Viperinae.
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100322
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Jaburetox: update on a urease-derived peptide J. Venom. Anim. Toxins incl. Trop. Dis.
Becker-Ritt,Arlete Beatriz; Portugal,Camila Saretta; Carlini,Célia Regina.
Abstract Urease from Canavalia ensiformis seeds was the first enzyme ever to be crystallized, in 1926. These proteins, found in plants, bacteria and fungi, present different biological properties including catalytic hydrolysis of urea, and also enzyme-independent activities, such as induction of exocytosis, pro-inflammatory effects, neurotoxicity, antifungal and insecticidal properties. Urease is toxic to insects and fungi per se but part of this toxicity relies on an internal peptide (~11 kDa), which is released upon digestion of the protein by insect enzymes. A recombinant form of this peptide, called jaburetox (JBTX), was constructed using jburell gene as a template. The peptide exhibits liposome disruption properties, and insecticidal and fungicidal...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Peptide; Bacteria; Membranes; Nanoparticles.
Ano: 2017 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992017000100211
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Proteolytic release and partial characterization of human sperm-surface glycopeptides BJMBR
Sperm-surface glycopeptides were obtained from intact sperm membranes after proteolytic release by different enzymatic treatments such as autoproteolysis, trypsin, papain and pronase. Glycopeptides were isolated, their properties and composition were examined, and their monosaccharide and amino acid constituents were characterized. The monosaccharides identified were fucose, mannose, galactose, N-acetylglucosamine, and N-acetylgalactosamine, which form part of more than one type of oligosaccharide units. Autoproteolytic treatment mainly provided O-glycosidic type oligosaccharides, while a mixture of O- and N-glycosidic oligosaccharides was obtained in variable proportions when treated with trypsin, papain or pronase. The highest degree of peptide cleavage...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Carbohydrate; Glycoconjugate; Proteolysis; Human sperm; Peptide.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000300013
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Stylicins, a new family of antimicrobial peptides from the Pacific blue shrimp Litopenaeus stylirostris ArchiMer
Rolland, Jean-luc; Abdelouahab, Mahdia; Dupont, J.; Lefevre, F.; Bachere, Evelyne; Romestand, Bernard.
The present study reports the characterization of Ls-Stylicin1, a novel antimicrobial peptide from the penaeid shrimp, Litopenoeus stylirostris. The predicted mature peptide of 82 residues is negatively charged (theoretical pl=5.0) and characterized by a proline-rich N-terminal region and a C-terminal region containing 13 cysteine residues. The recombinant Ls-Stylicin1 has been isolated in both monomeric and dimeric forms. Both display strong antifungal activity against Fusarium oxysporum (1.25 mu M < MIC <2.5 mu M), a pathogenic fungus of shrimp, but lower antimicrobial activity against Gram () bacteria, Vibrio sp. (40 mu M < MIC <80 mu M). However, rLs-Stylicin1 is able to agglutinate Vibrio pennaeicidae in vitro in agreement with its potent...
Tipo: Text Palavras-chave: Ls-Stylicin 1; Peptide; Shrimp; Antifungal; Agglutination; Vibrio.
Ano: 2010 URL: http://archimer.ifremer.fr/doc/00003/11387/8094.pdf
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