Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 8 de 8
Filtrar
Más filtros










Base de datos
Intervalo de año de publicación
1.
Food Res Int ; 143: 110286, 2021 05.
Artículo en Inglés | MEDLINE | ID: mdl-33992386

RESUMEN

Bioactive peptides have been broadly studied for their contribution to human health. This study aimed to identify bioactive peptides generated by in vitro gastrointestinal digestion of yam proteins. Yam protein concentrate (YPC) was submitted to simulated digestion. Gastric phase hydrolysate (GPH) and total gastrointestinal phase hydrolysate (GIPH) had their peptides identified by nanoLC-ESI-MS/MS. Peptide sequences were subjected to a database-driven (BIOPEP) bioactivity search. In vitro tests included: Antioxidant activity, DNA damage protection, ACE-inhibitory activity and antibacterial activity against the bacteria Escherichia coli, Salmonella sp. and Lysteria monocytogenes. Simulated digestion generated small peptides (mostly MW < 3500 Da), several of them with potential bioactive sequences predicted in silico. In both GPH and GIPH biological activities were detected, although GIPH displayed stronger DNA damage protection and antibacterial activity against Escherichia coli. The digestion of yam proteins releases promising biologically active peptides which can contribute to the prevention of bacterial infection and chronic degenerative diseases, with beneficial effects to human health.


Asunto(s)
Dioscorea , Secuencia de Aminoácidos , Digestión , Humanos , Péptidos , Espectrometría de Masas en Tándem
2.
Plant Foods Hum Nutr ; 75(3): 396-403, 2020 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-32462366

RESUMEN

Coconut antimicrobial peptide-1 (CnAMP1) is a naturally occurring bioactive peptide from green coconut water (Cocos nucifera L.). Although biological activities have been reported, the physiological relevance of these reports remains elusive as it is unknown if CnAMP1 is taken up into intestinal cells. To address this open question, we investigated the cytotoxicity of CnAMP1 in intestinal cells and its cellular uptake into human intestinal cells. Considering the importance of the P-glycoprotein (P-gp) to the intestinal metabolism of xenobiotics, we also investigated the influence of CnAMP1 on P-gp activity and expression. Both cell lines showed intracellular fluorescence after incubation with fluorescein labelled CnAMP1, indicating cellular uptake of the intact or fragmented peptide. CnAMP1 (12.5-400 µmol/L) showed no signs of cytotoxicity in LS180 and differentiated Caco-2 cells and did not affect P-gp expression and activity. Further research is required to investigate the identity of CnAMP1 hydrolysis fragments and their potential biological activities.


Asunto(s)
Miembro 1 de la Subfamilia B de Casetes de Unión a ATP , Cocos , Subfamilia B de Transportador de Casetes de Unión a ATP , Células CACO-2 , Humanos , Intestinos
3.
Curr Pharm Des ; 25(12): 1430-1439, 2019.
Artículo en Inglés | MEDLINE | ID: mdl-31124421

RESUMEN

ETHNOPHARMACOLOGICAL RELEVANCE: Mucuna pruriens (Mp) belongs to Leguminosae family, it is native of tropical regions and used to treat several maladies such as urinary, neurological, and menstruation disorders, constipation, edema, fever, tuberculosis, ulcers, diabetes, arthritis, dysentery, and cardiovascular diseases. Mp seeds are rich in bioactive compounds, for instance, lectins, a heterogeneous group of proteins and glycoproteins with a potential role as therapeutic tools for several conditions, including gastric disorders. This study investigated the acute toxicity, gastroprotective, and antioxidant activities of a lectin from Mucuna pruriens seeds (MpLec) on ethanol-induced gastropathy model in mice. MATERIAL AND METHODS: Mice received MpLec (5 or 10 mg/kg; i.v.) and were observed for acute toxicity signs; in another experimental series, mice were pre-treated with MpLec (0.001; 0.01 or 0.1 mg/kg, i.v.), ranitidine (80 mg/kg, p.o.), or saline (0.3 mL/30g, i.v.) before ethanol 99.9% (0.2 mL/animal, p.o.), and euthanized 30 min after ethanol challenge. Macroscopic and microscopic gastric aspects, biochemical parameters (tissue hemoglobin levels, iron-induced lipid peroxidation, GSH content, SOD activity, and gastric mucosal PGE2) were measured. Additionally, pharmacological tools (yohimbine, indomethacin, naloxone, L-NAME) were opportunely used to clarify MpLec gastroprotective mechanisms of action. RESULTS: No toxicity signs nor death were observed at acute toxicity tests. MpLec reduced ethanol-induced gastric damage, edema, and hemorrhagic patches formation, as well as decreased lipid peroxidation, SOD activity, and increased GSH content. Yohimbine and indomethacin prevented MpLec effects, suggesting the involvement of alpha-2 adrenoceptors and prostaglandins in the MpLec-mediated effects. CONCLUSION: MpLec does not present toxicity signs and shows gastroprotective and antioxidant activities via alpha-2 adrenoceptors and prostaglandins in the ethanol-induced gastropathy model.


Asunto(s)
Antioxidantes/farmacología , Mucosa Gástrica/efectos de los fármacos , Lectinas/farmacología , Mucuna/química , Prostaglandinas/metabolismo , Receptores Adrenérgicos/metabolismo , Úlcera Gástrica/terapia , Animales , Etanol/efectos adversos , Peroxidación de Lípido , Ratones , Fitoterapia , Extractos Vegetales/uso terapéutico , Semillas/química , Úlcera Gástrica/inducido químicamente , Pruebas de Toxicidad Aguda
4.
Int Immunopharmacol ; 38: 313-23, 2016 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-27344040

RESUMEN

Temporomandibular joint (TMJ) disorders show inflammatory components, heavily impacting on quality of life. Abelmoschus esculentus is largely cultivated in Northeastern Brazil for medicinal purposes, having it shown anti-inflammatory activity. We evaluated A. esculentus lectin (AEL) efficacy in reducing zymosan-induced temporomandibular joint inflammatory hypernociception in rats along with the mechanism of action through which it exerts anti-inflammatory activity. Animals were pre-treated with AEL (0.01, 0.1 or 1mg/kg) before zymosan (Zy) injection in the TMJ to determine anti-inflammatory activity. To analyse the possible effect of the hemeoxygenase-1 (HO-1) and the nitric oxide (NO) pathways on AEL efficacy, animals were pre-treated with ZnPP-IX (3mg/kg), a specific HO-1 inhibitor, or aminoguanidine (30mg/kg), a selective iNOS inhibitor, before AEL administration. Von Frey test evaluated inflammatory hypernociception, synovial fluid collection was performed to determine leukocyte counting and myeloperoxidase (MPO) activity 6h after Zy injection, and Evans Blue extravasation determined vascular permeability. TMJ tissue was collected for histopathological analysis (H&E) and immunohistochemistry (TNF-α, IL-1ß, HO-1). In addition, TMJ tissue and trigeminal ganglion collection was performed for TNF-α and IL-1ß dosage (ELISA). AEL increased inflammatory nociceptive threshold, reduced leukocyte influx along with MPO activity, leukocyte influx into the synovial membrane, and Evans Blue extravasation. It promoted HO-1 overexpression whilst decreased TNF-α and IL-1ß expression in the TMJ tissue. AEL reduced TNF-α and IL-1ß levels in TMJ tissue and trigeminal ganglion. AEL effects, however, were not observed in the presence of ZnPP-IX. These findings suggest that AEL efficacy depends on TNF-α/IL-1ß inhibition and HO-1 pathway integrity.


Asunto(s)
Abelmoschus/inmunología , Antiinflamatorios/uso terapéutico , Hemo-Oxigenasa 1/metabolismo , Inflamación/tratamiento farmacológico , Hipernutrición/tratamiento farmacológico , Lectinas de Plantas/uso terapéutico , Articulación Temporomandibular/efectos de los fármacos , Animales , Permeabilidad Capilar/efectos de los fármacos , Hemo-Oxigenasa 1/antagonistas & inhibidores , Inflamación/inducido químicamente , Interleucina-1beta/metabolismo , Masculino , Óxido Nítrico Sintasa de Tipo II/metabolismo , Hipernutrición/inducido químicamente , Protoporfirinas/farmacología , Ratas , Ratas Wistar , Transducción de Señal/efectos de los fármacos , Articulación Temporomandibular/patología , Factor de Necrosis Tumoral alfa/metabolismo , Zimosan
5.
Molecules ; 20(1): 348-57, 2014 Dec 26.
Artículo en Inglés | MEDLINE | ID: mdl-25549059

RESUMEN

Marine sponges are primitive metazoans that produce a wide variety of molecules that protect them against predators. In studies that search for bioactive molecules, these marine invertebrates stand out as promising sources of new biologically-active molecules, many of which are still unknown or little studied; thus being an unexplored biotechnological resource of high added value. Among these molecules, lectins are proteins that reversibly bind to carbohydrates without modifying them. In this review, various structural features and biological activities of lectins derived from marine sponges so far described in the scientific literature are discussed. From the results found in the literature, it could be concluded that lectins derived from marine sponges are structurally diverse proteins with great potential for application in the production of biopharmaceuticals, especially as antibacterial and antitumor agents.


Asunto(s)
Lectinas/química , Lectinas/farmacología , Biología Marina , Poríferos/química , Animales , Biotecnología
6.
PLoS One ; 9(3): e93361, 2014.
Artículo en Inglés | MEDLINE | ID: mdl-24675996

RESUMEN

The protein composition of goat milk differs between goat breeds and could present regional trends. The aim of this study was to comparatively analyze the protein composition of goat milk produced by the Alpine and Saanen breeds in northeastern Brazil and to evaluate the antibacterial activity of its protein fractions. SDS-PAGE, 2-DE electrophoresis and RP-HPLC analyses revealed the absence of αs1-casein in the milk of both breeds and no differences between the αs2-casein, ß-casein, ß-lactoglobulin and α-lactalbumin profiles. The amounts of soluble proteins and ß-casein hydrolysis residues were higher in Saanen milk. Only the protein fraction containing the largest amounts of casein (F60-90%) inhibited bacterial growth, with MIC values between 50 and 100 mg/mL. This study describe for the first time three important points about the goat milk protein of two Brazilian goat breeders: absence of α-s1 casein in the protein profile, differences between the milk protein composition produced by goats of Alpine and Saanen breeders and antibacterial activity of unbroken proteins (casein-rich fraction) present in these milk.


Asunto(s)
Antibacterianos/farmacología , Caseínas/farmacología , Lactalbúmina/farmacología , Leche/química , Animales , Antibacterianos/química , Antibacterianos/aislamiento & purificación , Bacillus subtilis/efectos de los fármacos , Bacillus subtilis/crecimiento & desarrollo , Brasil , Cruzamiento , Caseínas/química , Caseínas/aislamiento & purificación , Escherichia coli/efectos de los fármacos , Escherichia coli/crecimiento & desarrollo , Femenino , Cabras , Hidrólisis , Lactalbúmina/química , Lactalbúmina/aislamiento & purificación , Masculino , Pruebas de Sensibilidad Microbiana , Pseudomonas aeruginosa/efectos de los fármacos , Pseudomonas aeruginosa/crecimiento & desarrollo , Staphylococcus aureus/efectos de los fármacos , Staphylococcus aureus/crecimiento & desarrollo
7.
Protein J ; 31(8): 674-80, 2012 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-22965555

RESUMEN

The Abelmoschus esculentus (Malvaceae) plant originated in Africa and has spread across a number of tropic countries, including northeastern Brazil. The plant has been used to treat various disorders, such as cancer, microbial infections, hypoglycemia, constipation, urine retention and inflammation. The lectin of A. esculentus (AEL) was isolated by precipitation with ammonium sulfate at a saturation level of 30/60 and purified by ion exchange chromatography (Sephacel-DEAE). The electrophoresis (SDS-PAGE) profile of the AEL showed two protein bands of apparent molecular mass of approximately 15.0 and 21.0 kDa. The homogenity of the protein was confirmed by electrospray mass spectrometry (ESI-MS), which revealed the presence of a 10.29-kDa monomer and a 20.58-kDa dimer. The AEL exhibits agglutinating activity against rabbit (74.41 UH/mP) and human type ABO erythrocytes (21.00 UH/mP). This activity does not require the presence of divalent cations and is specifically inhibited by lactose, fructose and mannose. The intravenous treatment with 0.01, 0.1 and 1 mg/kg of AEL inhibited the paw edema elicited by carrageenan by approximately 15, 22 and 44 %, respectively, but not that induced by dextran. In addition, treatment with 0.1, 1 and 10 mg/kg of AEL also inhibited the abdominal writhing induced by acetic acid by approximately 52, 57 and 69 %, respectively. In conclusion, AEL is a new lectin with a molecular mass of 20.0 kDa, which is -composed of a 10.291-Da monomer and a 20.582-kDa dimer, that exhibits anti-inflammatory, antinociceptive and hemagglutinating activities. In addition, the lectin hemagglutinating property is both metallo-independent and associated with the lectin domain.


Asunto(s)
Abelmoschus/química , Analgésicos/aislamiento & purificación , Analgésicos/farmacología , Antiinflamatorios/aislamiento & purificación , Antiinflamatorios/farmacología , Lectinas de Plantas/aislamiento & purificación , Lectinas de Plantas/farmacología , Ácido Acético , Analgésicos/química , Análisis de Varianza , Animales , Antiinflamatorios/química , Metabolismo de los Hidratos de Carbono , Carragenina/efectos adversos , Edema/inducido químicamente , Agregación Eritrocitaria/efectos de los fármacos , Femenino , Pruebas de Hemaglutinación , Humanos , Inflamación/inducido químicamente , Masculino , Ratones , Dimensión del Dolor/efectos de los fármacos , Lectinas de Plantas/química , Conejos , Ratas , Ratas Wistar , Semillas/química
8.
Biochem Biophys Res Commun ; 350(4): 1050-5, 2006 Dec 01.
Artículo en Inglés | MEDLINE | ID: mdl-17045568

RESUMEN

This paper describes the purification and characterization of a new N-acetyl-d-glucosamine-specific lectin from Araucaria angustifolia (AaL) seeds (Araucariaceae) and its anti-inflammatory and antibacterial activities. AaL was purified using a combination of affinity chromatography on a chitin column and ion exchange chromatography on Sephacel-DEAE. The pure protein has 8.0kDa (SDS-PAGE) and specifically agglutinates rabbit erythrocytes, effect that was independent of the presence of divalent cations and was inhibited after incubation with glucose and N-acetyl-d-glucosamine. AaL showed antibacterial activity against Gram-negative and Gram-positive strains, shown by scanning electron microscopy. AaL, intravenously injected into rats, showed anti-inflammatory effect, via carbohydrate site interaction, in the models of paw edema and peritonitis. This lectin can be used as a tool for studying bacterial infections and inflammatory processes.


Asunto(s)
Bacterias/citología , Bacterias/efectos de los fármacos , Cycadopsida/metabolismo , Inflamación/tratamiento farmacológico , Lectinas de Plantas/administración & dosificación , Semillas/química , Animales , Relación Dosis-Respuesta a Droga , Extractos Vegetales/administración & dosificación , Extractos Vegetales/aislamiento & purificación , Lectinas de Plantas/aislamiento & purificación , Ratas
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA
...