beta-Lactoglobulin (beta-LG) is one of the cow's major milk proteins and the most abundant whey protein. This globular protein of about 18 kDa is folded, forming a beta-barrel (or calyx) structure. This structure is stabilized by two disulfide bonds and can be altered by heating above 65 degrees C. beta-LG is also one of the major allergens in milk. Heating is one of the most common technologic treatments applied during many milk transformations. During heating in the presence of reducing sugars, beta-LG is also submitted to the Maillard reaction, which at the first stage consists of the covalent fixation of sugars on the epsilon-amino groups of lysyl residues. The following steps are condensation and polymerization reactions leading to the formation of melanoidins (brown pigments). Despite the frequency of use of heating during milk transformation, the effects of heat-induced denaturation and of glycation of beta-LG on its recognition by IgE from cow's milk allergy (CMA) patients are not fully understood. The objectives of our work were to evaluate the effect of heat-induced denaturation of bovine beta-LG on binding of IgE from CMA patients and to determine the effect of moderate glycation on the degree of recognition by IgE. We showed that heat-induced denaturation (loss of tertiary and secondary structures) of beta-LG is associated with weaker binding of IgE from CMA patients. It was also shown that moderate glycation of beta-LG in early stages of Maillard reaction has only a small effect on its recognition by IgE, whereas a high degree of glycation has a clear "masking" effect on the recognition of epitopes. This demonstrates the importance of epsilon-amino groups of lysines in the definition of epitopes recognized by IgE.
Gemini surfactants have important advantages, e.g., low micromolar CMCs and slow millisecond monomer ↔ micelle kinetics, for membrane mimetics and for delivering nucleic acids for gene therapy or RNA silencing. However, as a prerequisite, it is important to characterize interactions occurring between Gemini surfactants and proteins. Here NMR and CD spectroscopies are employed to investigate the interactions of cationic Gemini surfactants with RNase Sa, a negatively charged ribonuclease. We find that RNase Sa binds Gemini surfactant monomers and micelles at pH values above 4 to form aggregates. Below pH 4, where the protein is positively charged, these aggregates dissolve and interactions are undetectable. Thermal denaturation experiments show that surfactant lowers RNase Sa's conformational stability, suggesting that surfactant binds the protein's denatured state preferentially. Finally, Gemini surfactants were found to bind RNA, leading to the formation of large complexes. Interestingly, Gemini surfactant binding did not prevent RNase Sa from cleaving RNA.
A simple and eco-friendly method for efficient synthesis of stable colloidal silver nanoparticles (AgNPs) using extracts is described. A series of reactions was conducted using different types and concentrations of plant extract as well as metal ions to optimize the reaction conditions. AgNPs were characterized by using UV-vis spectroscopy, transmission electron microscopy, atomic force microscopy, dynamic light scattering, zetasizer, energy-dispersive X-ray spectroscopy (EDAX) and Fourier transform infrared spectroscopy (FTIR). At the optimized conditions, plate shaped AgNPs with zeta potential value of -15.7 and plasmon absorption maximum at 450 nm were obtained using high concentration of aqueous extract. Efficient adsorption of organic compounds on the nanoparticles was confirmed by FTIR and EDAX. The biogenic AgNPs displayed promising antibacterial activity on, , and. The highest antibacterial activity of 25 µg mL-1 was obtained for all the strains using aqueous extract synthesized AgNPs. The aqueous extract synthesised AgNPs also showed considerable antifungal activity against fluconazole resistant . The cytotoxicity assay revealed considerable anticancer activity of AgNPs on HeLa and MCF-7 cancer cells. Overall results indicated high potential of extract to synthesis high quality AgNPs for biomedical applications.
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