ovalbumin and caffeic-acid

With the increasing demand for functional foods, the study on binding of active molecules and ovalbumin (OVA) via weak interaction has attracted widespread attention. In this work, the interaction mechanism of OVA and caffeic acid (CA) was revealed using fluorescence spectroscopy and dynamics simulation. The CA-induced fluorescence decrease of OVA was static quenching. Their binding complex had about 1 binding site and a 3.39 × 10

Topics: Binding Sites; Molecular Docking Simulation; Molecular Dynamics Simulation; Ovalbumin; Protein Binding; Spectrometry, Fluorescence

Caffeic amides are derivatives of caffeic acid, which have antioxidant and anti-inflammatory properties, and high in vivo stability. The therapeutic effect of caffeic amides on allergic diseases, and especially on the maturation of bone marrow-derived dendritic cells (BM-DCs), remains unclear. In this study, we investigated the therapeutic potential of caffeic amides on allergic diseases by evaluating the maturation of DCs and evaluated their potential in inducing the differentiation of T. BM-DCs isolated from BALB/c mice were treated with different caffeic amide derivatives for 48 h and the expression of surface markers was analyzed by flow cytometry. The differentiation of CD4. Our results showed that among the six caffeic amides tested herein, only 36 M significantly inhibited the antigen-induced maturation of DCs associated with the expression of CD80, CD86, and major histocompatibility complex II (VC ovalbumin (OVA)+ thymic stromal lymphopoietin (TSLP) vs. 36 M OVA + TSLP). Additionally, the isolation and co-culture of antigen-specific CD4. Among the six caffeic amides tested herein, 36 M (N-octyl caffeamide) might possess therapeutic potential for allergic diseases.

Topics: Allergens; Amides; Animals; Anti-Allergic Agents; Bone Marrow Cells; Caffeic Acids; Cell Differentiation; Cytokines; Dendritic Cells; Disease Models, Animal; Female; Flow Cytometry; Hypersensitivity; Mice; Mice, Inbred BALB C; Ovalbumin; Thymic Stromal Lymphopoietin

Ovalbumin (OVA) is described as one of the major allergens in hen's egg, and it is the most abundant protein in egg white. Enzyme-mediated covalent cross-linking of food proteins, can influence their structure and allergenicity. The aim of this study was to investigate the potential of polyphenol oxidase from Agaricus bisporus to cross-link OVA (CL-OVA) in the presence or absence of caffeic acid, followed by characterizing the structure and allergenicity of CL-OVA. A single-factor experiment was designed to assess the optimum conditions for cross-linking of OVA by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Under the optimal conditions, structural changes in OVA were analyzed by circular dichroism, ultraviolet and fluorescence spectra. It was shown that CL-OVA became unordered and unfolded, and more tyrosine and tryptophan residues and hydrophobic groups were exposed onto the surface of molecules when compared to the native OVA. Enzyme-linked immunosorbent assay indicated that IgG and IgE binding abilities to OVA significantly reduced after cross-linking. All the findings demonstrated that enzymatic cross-linking in the presence of caffeic acid as a mediator may decrease the antigenicity and potential allergenicity, and the changes of the modified OVA were most likely a consequence of some changes or adjustment in the local conformation of OVA and the epitopes of OVA by cross-linking.

Topics: Adult; Allergens; Biocatalysis; Caffeic Acids; Catechol Oxidase; Child; Child, Preschool; Circular Dichroism; Cross-Linking Reagents; Female; Humans; Hydrogen-Ion Concentration; Immunoglobulin E; Immunoglobulin G; Infant; Male; Osmolar Concentration; Ovalbumin; Protein Structure, Secondary; Temperature; Time Factors

Clerodendron trichotomum leaves and Rumex aquatica herbs are used as a folk medicine for the treatment of inflammatory diseases, but their active ingredients are not known until now. We isolated caffeic acid and phenylpropanoid glycosides, 1-O-caffeoyl glycoside and acteoside [β-(3',4'-dihydroxyphenyl) ethyl-O-α-l-rhamnopyranosyl(1→3)-β-d-(4-O-caffeoyl)-glucopyranoside] from their ethylacetate fractions, respectively, and evaluated their anti-asthmatic effects on the aerosolized ovalbumin (OA) challenge in the OA-sensitized guinea-pigs measuring the specific airway resistance (sRaw) during the immediate-phase response (IAR) and late-phase response (LAR), and also measured recruitment of leukocytes and chemical mediators on the bronchoalveolar lavage fluids (BALF) in LAR, as well as histopathological survey. Acteoside and 1-O-caffeoyl glycoside (25mg/kg) significantly (P<0.05) inhibited sRaw by 32.14 and 26.79% in IAR, and by 55.88% and 52.94% in LAR, respectively, whereas caffeic acid (25mg/kg) inhibited sRaw by 30.36% in IAR and 44.12% in LAR, compared to control, but with less effective than dexamethasone, disodium cromoglycate, and salbutamol, respectively. In addition, phenylpropanoid glycosides (25mg/kg) significantly inhibited the recruitments of leukocytes, particularly neutrophils and eosinophils into lung, Furthermore, 1-O-caffeoyl glycoside, acteoside and caffeic acid significantly (P<0.05) inhibited protein content at a dose of 25mg/kg, and histamine content and PLA(2) activity at a dose of 50mg/kg, in BALF. Acteoside had more active than caffeic acid and 1-O-caffeoyl glycoside. However, their anti-asthmatic effects were less than the reference drugs. These results indicated that caffeic acid and its glycosides (25mg/kg) have anti-asthmatic effect as the same manner with dexamethasone and disodium cromoglycate.

Topics: Airway Resistance; Albuterol; Animals; Anti-Asthmatic Agents; Asthma; Bronchoalveolar Lavage Fluid; Caffeic Acids; Clerodendrum; Cromolyn Sodium; Dexamethasone; Glucosides; Glycosides; Guinea Pigs; Histamine; Leukocytes; Lung; Male; Neutrophil Infiltration; Ovalbumin; Phenols; Phytotherapy; Plant Extracts; Plant Leaves; Propanols; Proteins; Rumex