Influence of heterogeneity biocolloids surface on their electrophoretic separation

Electrical properties of biocolloids, due to the unique structure and properties of the walls and cell membranes are altered by ions present in the environment. This change in the surface properties of bacterial cells has a major impact on the effects of cell-cell or cell-surface during the formation of aggregates or biofilm. Each microorganism has a complex and characteristic cell wall composition, which surface charge originates from the ionization of carboxyl, phosphate or amino groups and the adsorption of ions from solution. Consequently, the charged cell wall groups determine the spontaneous formation of the electrical double layer (EDL). The properties of the EDL affect the behavior of biocolloid including cell-to-cell and cell-to-capillary surface interactions. In addition, the inner wall surface of capillary groups (modified and/or unmodified) interact with the solvent and the analyte. Biocolloids effect of aggregation and adhesion to the surface of the capillary is unfavorable phenomenon occurring during the electrophoretic separation. These phenomena are highly correlated with the acid-base properties of the bacterial cells. Interactions between molecules are unstable, hence the analytes adsorbed on the surface concerned can be removed using a variety of solvents or physico-chemical and mechanical factors. However, when the bacterial cells are in close proximity to the charged surface of the capillary may be subject to specific and non-specific short-range interactions, which are characterized by high stability. It has been shown the characteristics of the microbial surface in order to determine their role in adhesion and aggregation phenomena during the electrophoretic separation. The use of experimental techniques, including instrumental, electrochemical and electrophoretic allowed the description of the relationship between the acid-base properties of pathogens and their behavior. The review summarizes the research on biocolloids which are helpful in understanding the interactions that occur during electrophoretic analysis

Food quality control by hyphenated separation techniques

Food as complex mixture of proteins, lipids, vitamins, etc. cannot be separated and identified by using in only one method. This article presents a revision on the hyphenated chromatographic techniques and methods used in food analysis and described main application in food science research, and determination of xenobiotics and their metabolites in environmental. Also article discusses applications of “omics” in food analysis (proteomics, transcriptomics, genomics, metabolomis) and new discipline of – foodomics

Mechanistic chromatographic column characterization for the analysis of flavonoids using quantitative structure?retention relationships based on density functional theory

10.3390/ijms21062053International Journal of Molecular Sciences216205

Study on zinc ions binding to the individual casein fractions: αS1-, β- and κ-casein.

The presented work is focused on the isotherm study on the Zn2+ ions binding to the individual casein fractions: αS1-, β- and κ-casein (αS1CN, βCN and κCN). The experimental isotherms were evaluated using Freundlich and Langmuir models. Subsequently, the stability of the obtained complexes in the respective Zn2+ ion concentrations (120, 350, 600 mg/L) was determined by carrying out zeta potential measurements. Capillary electrophoresis combined with inductively coupled plasma mass spectrometry (CE-ICP-MS) confirmed the occurring binding process. Additionally, physicochemical characteristics of the obtained metal-protein complexes was performed including scanning electron microscopy (SEM) in two modes (SE and Z-contrast) and the binding sites of caseins to Zn2+ ions were indicated using attenuated total reflectance infrared spectroscopy (FTIR-ATR) and Raman analysis as well as mass spectrometry technique (MALDI-TOF MS). Isothermal studies indicated a heterogeneously complex zinc ion adsorption process, and a stability study showed that the zeta potential is strongly related to the hydrophobicity, size and structure of the casein isoforms studied. Electron microscopy confirmed the modification of casein surfaces due to the addition of Zn2+ ions. Spectroscopic techniques indicated the interaction of zinc ions with polar amino acids of casein, such as glutamic acid (Glu) and aspartic acid (Asp), but also His, Cys. The influence of phosphate groups was also observed. Finally, the study culminated in a molecular docking study of the Zn2+ ion binding process, which confirmed the presence of the listed amino acids responsible for the binding process

Synthesis, physicochemical characterization, and antibacterial performance of silver-lactoferrin complexes.

Antibiotic-resistant bacteria pose one of the major threats to human health worldwide. The issue is fundamental in the case of chronic wound treatment. One of the latest trends to over-come the problem is the search for new antibacterial agents based on silver. Thus, the aim of this research was to synthesize the silver-lactoferrin complex as a new generation of substances for the treatment of infected wounds. Moreover, one of the tasks was to investigate the formation mechanisms of the respective complexes and the influence of different synthesis conditions on the features of final product. The batch-sorption study was performed by applying the Langmuir and Freun-dlich isotherm models for the process description. Characterization of the complexes was carried out by spectroscopy, spectrometry, and separation techniques, as well as with electron microscopy. Additionally, the biological properties of the complex were evaluated, i.e., the antibacterial activity against selected bacteria and the impact on L929 cell-line viability. The results indicate the formation of a heterogeneous silver–lactoferrin complex that comprises silver nanoparticles. The complex has higher antibacterial strength than both native bovine lactoferrin and Ag+, while being comparable to silver toxicity

Target-based drug discovery through inversion of quantitative structure-drug-property relationships and molecular simulation: CA IX-sulphonamide complexes

In this work, a target-based drug screening method is proposed exploiting the synergy effect of ligand-based and structure-based computer-assisted drug design. The new method provides great flexibility in drug design and drug candidates with considerably lower risk in an efficient manner. As a model system, 45 sulphonamides (33 training, 12 testing ligands) in complex with carbonic anhydrase IX were used for development of quantitative structure-activity-lipophilicity (property)-relationships (QSPRs). For each ligand, nearly 5,000 molecular descriptors were calculated, while lipophilicity (logkw) and inhibitory activity (logKi) were used as drug properties. Genetic algorithm-partial least squares (GA-PLS) provided a QSPR model with high prediction capability employing only seven molecular descriptors. As a proof-of-concept, optimal drug structure was obtained by inverting the model with respect to reference drug properties. 3509 ligands were ranked accordingly. Top 10 ligands were further validated through molecular docking. Large-scale MD simulations were performed to test the stability of structures of selected ligands obtained through docking complemented with biophysical experiments

Detection of plant protein adulterated in fluid milk using two-dimensional gel electrophoresis combined with mass spectrometry

peer reviewedThe illegal or unlabelled addition of plant protein in milk can cause serious anaphylaxis. For sustainable food security, it is therefore important to develop a methodology to detect non-milk protein in milk products. This research aims to differentiate milk adulterated with plant protein using two-dimensional gel electrophoresis (2-DE) coupled with mass spectrometry. According to the protein spots highlighted on the gel of adulterated milk,b-conglycinin and glycinin were detected in milk adulterated with soy protein, while legumin, vicilin, and convicilin indicated the addition of pea protein, and b-amylase and serpin marked wheat protein. These results suggest that a 2-DE-based protein profile is a useful method to identify milk adulterated with soy and pea protein, with a detection limit of 4% plant protein in the total protein