LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Erweiterte Suche

Suchergebnis

Treffer 1 - 5 von insgesamt 5

Suchoptionen

  1. Artikel: LC-ESI-IT-MS/MS and MALDI-TOF Approach: Identification of Natural Polymers from Rhizophora mangle Barks and Determination of Their Analgesic and Anti-inflammatory Properties.

    de Souza Mesquita, Leonardo Mendes / Rodrigues, Caroline Fabri Bittencourt / da Rocha, Cláudia Quintino / Bianchim, Mayara Silveira / Rodrigues, Clenilson Martins / de Oliveira, Vanda Maria / Gaeta, Henrique Hessel / Belchor, Mariana Novo / Toyama, Marcos Hikari / Vilegas, Wagner

    Natural products and bioprospecting

    2018  Band 9, Heft 1, Seite(n) 23–34

    Abstract: We recognize the chemical composition of the acetonic extract of Rhizophora mangle barks (AERM) using mass spectrometry analysis [liquid chromatography (LC)-ESI-IT-MS/MS and matrix-assisted laser desorption/ionization-time of flight-MS (MALDI-TOF)]. ... ...

    Abstract We recognize the chemical composition of the acetonic extract of Rhizophora mangle barks (AERM) using mass spectrometry analysis [liquid chromatography (LC)-ESI-IT-MS/MS and matrix-assisted laser desorption/ionization-time of flight-MS (MALDI-TOF)]. Analgesic activity was evaluated by formalin and tail-flick experimental assays. Anti-inflammatory activity was performed by paw edema test induced by carrageenan and 48/80 compounds. The first series of experiments involved [LC]-FIA-IT-MS/MS with 11 separated catechins derivatives until degree of polymerization 3 (DP3). The spectra obtained by MALDI-TOF analysis of the AERM presented two homologous series: one based on polymers of m/z 288 Da increments (up to DP12) and another series based on polymers of m/z [288 + 162] Da increments (up to DP11). In addition to these series of flavan-3-ol, each DP had a subset of masses with a variation of - 16 Da (homologous series of afzelechins-m/z 873-3465 Da) and + 16 Da (homologous series of gallocatechins-m/z 905-3497 Da). A similar pattern with homologous series of gallocatechins and afzelechins could also be observed for a fifth and a sixth monohexoside series: glucogallocatechins (m/z 779-3371) and glucoafzelechins (m/z 747-3339). The intraperitoneal administration of different doses of AERM (50, 150 and 300 µg mL
    Sprache Englisch
    Erscheinungsdatum 2018-11-14
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ISSN 2192-2195
    ISSN 2192-2195
    DOI 10.1007/s13659-018-0192-8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  2. Artikel ; Online: Purification and characterization of the first γ-phospholipase inhibitor (γPLI) from Bothrops jararaca snake serum.

    Serino-Silva, Caroline / Morais-Zani, Karen / Hikari Toyama, Marcos / Toyama, Daniela de Oliveira / Gaeta, Henrique Hessel / Rodrigues, Caroline Fabri Bittencourt / Aguiar, Wéslei da Silva / Tashima, Alexandre Keiji / Grego, Kathleen Fernandes / Tanaka-Azevedo, Anita Mitico

    PloS one

    2018  Band 13, Heft 3, Seite(n) e0193105

    Abstract: Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty acids and lysophospholipids and deconstructing the cell membrane. This protein is commonly found in snake venoms, causing tissue inflammation in the ... ...

    Abstract Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty acids and lysophospholipids and deconstructing the cell membrane. This protein is commonly found in snake venoms, causing tissue inflammation in the affected area. Evidence indicates that snakes have natural resistance to their own venom due to protective properties in plasma, that inhibit the action of proteins present in their venom. Given that, this study aimed to purify and characterize a γPLI from Bothrops jararaca serum, named γBjPLI. PLA2 inhibitor was isolated using two chromatographic steps: an ion exchange column (DEAE), followed by an affinity column (crotoxin coupled to a CNBr-activated Sepharose resin). The purity and biochemical characterization of the isolated protein were analyzed by RP-HPLC, SEC, SDS-PAGE, circular dichroism and mass spectrometry. The ability to inhibit PLA2 was determined by enzymatic activity, neutralization of paw edema and myonecrosis. The protein purity was confirmed by RP-HPLC and SEC, whilst an apparent molecular mass of 25 kDa and 20 kDa was obtained by SDS-PAGE, under reducing and non-reducing conditions, respectively. According to mass spectrometry analysis, this protein showed 72% and 68% of coverage when aligned to amino acid sequences of two proteins already described as PLIs. Thus, the inhibitory activity of enzymatic, edema and myonecrotic activities by γBjPLI suggests a role of this inhibitor for protection of these snakes against self-envenomation.
    Mesh-Begriff(e) Animals ; Blood Proteins/chemistry ; Blood Proteins/genetics ; Blood Proteins/isolation & purification ; Blood Proteins/metabolism ; Bothrops/blood ; Phospholipase A2 Inhibitors/blood ; Phospholipase A2 Inhibitors/chemistry ; Phospholipase A2 Inhibitors/isolation & purification ; Phospholipases A2 ; Reptilian Proteins/blood ; Reptilian Proteins/chemistry ; Reptilian Proteins/genetics ; Reptilian Proteins/isolation & purification
    Chemische Substanzen Blood Proteins ; Phospholipase A2 Inhibitors ; Reptilian Proteins ; Phospholipases A2 (EC 3.1.1.4)
    Sprache Englisch
    Erscheinungsdatum 2018
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0193105
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  3. Artikel ; Online: Evaluation of Potential Thrombin Inhibitors from the White Mangrove (Laguncularia racemosa (L.) C.F. Gaertn.).

    Rodrigues, Caroline Fabri Bittencourt / Gaeta, Henrique Hessel / Belchor, Mariana Novo / Ferreira, Marcelo José Pena / Pinho, Marcus Vinícius Terashima / Toyama, Daniela de Oliveira / Toyama, Marcos Hikari

    Marine drugs

    2015  Band 13, Heft 7, Seite(n) 4505–4519

    Abstract: The aim of this work was to verify the effects of methanol (MeOH) and hydroalcoholic (HA) extracts and their respective partition phases obtained from white mangrove (Laguncularia racemosa (L.) C.F. Gaertn.) leaves on human thrombin activity. Among the ... ...

    Abstract The aim of this work was to verify the effects of methanol (MeOH) and hydroalcoholic (HA) extracts and their respective partition phases obtained from white mangrove (Laguncularia racemosa (L.) C.F. Gaertn.) leaves on human thrombin activity. Among the extracts and phases tested, only the ethyl acetate and butanolic partitions significantly inhibited human thrombin activity and the coagulation of plasma in the presence of this enzyme. Chromatographic analyses of the thrombin samples incubated with these phases revealed that different compounds were able to interact with thrombin. The butanolic phase of the MeOH extract had the most potent inhibitory effects, reducing enzymatic activity and thrombin-induced plasma coagulation. Two glycosylated flavonoids in this partition were identified as the most potent inhibitors of human thrombin activity, namely quercetin-3-O-arabinoside (QAra) and quercetin-3-O-rhamnoside (Qn). Chromatographic analyses of thrombin samples incubated with these flavonoids demonstrated the chemical modification of this enzyme, suggesting that the MeOH extract contained other compounds that both induced structural changes in thrombin and diminished its activity. In this article, we show that despite the near absence of the medical use of mangrove compounds, this plant contains natural compounds with potential therapeutic applications.
    Mesh-Begriff(e) Blood Coagulation/drug effects ; Chromatography, High Pressure Liquid ; Combretaceae/chemistry ; Flavonoids/isolation & purification ; Flavonoids/pharmacology ; Humans ; Plant Extracts/isolation & purification ; Plant Extracts/pharmacology ; Plant Leaves/chemistry ; Thrombin/antagonists & inhibitors
    Chemische Substanzen Flavonoids ; Plant Extracts ; Thrombin (EC 3.4.21.5)
    Sprache Englisch
    Erscheinungsdatum 2015-07-21
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2175190-0
    ISSN 1660-3397 ; 1660-3397
    ISSN (online) 1660-3397
    ISSN 1660-3397
    DOI 10.3390/md13074505
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  4. Artikel ; Online: Evaluation of macroalgae sulfated polysaccharides on the Leishmania (L.) amazonensis promastigote.

    Lehnhardt Pires, Camila / Rodrigues, Selma Dzimidas / Bristot, Daniel / Gaeta, Henrique Hessel / de Oliveira Toyama, Daniela / Lobo Farias, Wladimir Ronald / Toyama, Marcos Hikari

    Marine drugs

    2013  Band 11, Heft 3, Seite(n) 934–943

    Abstract: The sulfated polysaccharides from Solieria filiformis (Sf), Botryocladia occidentalis (Bo), Caulerpa racemosa (Cr) and Gracilaria caudata (Gc) were extracted and extensively purified. These compounds were then subjected to in vitro assays to evaluate the ...

    Abstract The sulfated polysaccharides from Solieria filiformis (Sf), Botryocladia occidentalis (Bo), Caulerpa racemosa (Cr) and Gracilaria caudata (Gc) were extracted and extensively purified. These compounds were then subjected to in vitro assays to evaluate the inhibition of these polysaccharides on the growth of Leishmania (L.) amazonensis promastigotes. Under the same assay conditions, only three of the four sulfated polysaccharides were active against L. amazonensis, and the polysaccharide purified from Cr was the most potent (EC50 value: 34.5 μg/mL). The polysaccharides derived from Bo and Sf demonstrated moderate anti-leishmanial activity (EC50 values of 63.7 μg/mL and 137.4 μg/mL). In addition, we also performed in vitro cytotoxic assays toward peritoneal macrophages and J774 macrophages. For the in vitro cytotoxicity assay employing J774 cells, all of the sulfated polysaccharides decreased cell survival, with CC50 values of 27.3 μg/mL, 49.3 μg/mL, 73.2 μg/mL, and 99.8 μg/mL for Bo, Cr, Gc, and Sf, respectively. However, none of the sulfated polysaccharides reduced the cell growth rate of the peritoneal macrophages. These results suggest that macroalgae contain compounds with various chemical properties that can control specific pathogens. According to our results, the assayed sulfated polysaccharides were able to modulate the growth rate and cell survival of Leishmania (L.) amazonensis promastigotes in in vitro assays, and these effects involved the interaction of the sulfated polysaccharides on the cell membrane of the parasites.
    Mesh-Begriff(e) Animals ; Antiprotozoal Agents/chemistry ; Antiprotozoal Agents/isolation & purification ; Antiprotozoal Agents/pharmacology ; Cell Line ; Cell Membrane/drug effects ; Cell Membrane/parasitology ; Cell Survival/drug effects ; Leishmania/drug effects ; Macrophages/drug effects ; Macrophages/metabolism ; Macrophages, Peritoneal/drug effects ; Macrophages, Peritoneal/metabolism ; Polysaccharides/chemistry ; Polysaccharides/isolation & purification ; Polysaccharides/pharmacology ; Seaweed/chemistry ; Sulfates/chemistry
    Chemische Substanzen Antiprotozoal Agents ; Polysaccharides ; Sulfates
    Sprache Englisch
    Erscheinungsdatum 2013-03-20
    Erscheinungsland Switzerland
    Dokumenttyp Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2175190-0
    ISSN 1660-3397 ; 1660-3397
    ISSN (online) 1660-3397
    ISSN 1660-3397
    DOI 10.3390/md11030934
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

  5. Artikel ; Online: An evaluation of 3-rhamnosylquercetin, a glycosylated form of quercetin, against the myotoxic and edematogenic effects of sPLA 2 from Crotalus durissus terrificus.

    Toyama, Daniela de Oliveira / Gaeta, Henrique Hessel / de Pinho, Marcus Vinícius Terashima / Ferreira, Marcelo José Pena / Romoff, Paulete / Matioli, Fábio Filippi / Magro, Angelo José / Fontes, Marcos Roberto de Mattos / Toyama, Marcos Hikari

    BioMed research international

    2014  Band 2014, Seite(n) 341270

    Abstract: This paper shows the results of quercitrin effects on the structure and biological activity of secretory phospholipase (sPLA2) from Crotalus durissus terrificus, which is the main toxin involved in the pharmacological effects of this snake venom. ... ...

    Abstract This paper shows the results of quercitrin effects on the structure and biological activity of secretory phospholipase (sPLA2) from Crotalus durissus terrificus, which is the main toxin involved in the pharmacological effects of this snake venom. According to our mass spectrometry and circular dichroism results, quercetin was able to promote a chemical modification of some amino acid residues and modify the secondary structure of C. d. terrificus sPLA2. Moreover, molecular docking studies showed that quercitrin can establish chemical interactions with some of the crucial amino acid residues involved in the enzymatic activity of the sPLA2, indicating that this flavonoid could also physically impair substrate molecule access to the catalytic site of the toxin. Additionally, in vitro and in vivo assays showed that the quercitrin strongly diminished the catalytic activity of the protein, altered its Vmax and Km values, and presented a more potent inhibition of essential pharmacological activities in the C. d. terrificus sPLA2, such as its myotoxicity and edematogenic effect, in comparison to quercetin. Thus, we concluded that the rhamnose group found in quercitrin is most likely essential to the antivenom activities of this flavonoid against C. d. terrificus sPLA2.
    Mesh-Begriff(e) Animals ; Circular Dichroism ; Crotalid Venoms/chemistry ; Crotalid Venoms/isolation & purification ; Crotalid Venoms/toxicity ; Crotalus/metabolism ; Edema/pathology ; Enzyme Assays ; Glycosylation/drug effects ; Male ; Mice ; Molecular Docking Simulation ; Muscle Cells/drug effects ; Muscle Cells/pathology ; Phospholipases A2, Secretory/chemistry ; Phospholipases A2, Secretory/isolation & purification ; Phospholipases A2, Secretory/toxicity ; Quercetin/analogs & derivatives ; Quercetin/chemistry ; Quercetin/pharmacology
    Chemische Substanzen Crotalid Venoms ; quercitrin (2Y8906LC5P) ; Quercetin (9IKM0I5T1E) ; Phospholipases A2, Secretory (EC 3.1.1.4)
    Sprache Englisch
    Erscheinungsdatum 2014-02-18
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2698540-8
    ISSN 2314-6141 ; 2314-6133
    ISSN (online) 2314-6141
    ISSN 2314-6133
    DOI 10.1155/2014/341270
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

Zum Seitenanfang