The aim was to evaluate the structural similarity of the protein - GCSF – in different isolates and in the originator commercial product. The study based on the recombinant synthesis, NMR, and cheminformatics, was designed to build a methodology for the development and registration of biopharmaceuticals. The criteria to determine the identity or degree of similarity of selected spectral regions of the proteins are selected to help optimizing the controllable parameters of the production technology and to argument the identity of the new isolate with the originator.
COBISS.SI-ID: 3725082
The liver cell membrane transport of flavonols and anthocyanins through the membrane protein bilitranslocase was investigated. It was found that binding relies on the ability to establish hydrogen bonds, ruling out the involvement of charge interactions. This conclusion was drawn on the basis of the model developed with selected structural descriptors. The results show that most of the flavonols, contrary to anthocyanins, do not react with bilitranslocase, except for some aglycones that show weak interaction.
COBISS.SI-ID: 3622426
We explored the sensitivity of numerical characterizations of proteome on the number of proteins considered. We examined data on proteomics maps belonging to the liver cells of mice subject to four proliferators. The number of proteins considered for quantitative analysis was varied from 25 up to 1000 proteins. We have compared the similarity/dissimilarity results when different number of proteins has been considered. We found that proteins maps based on a set of about 300 most abundant proteins spots suffice for satisfactory numerical characterization of corresponding proteome.
COBISS.SI-ID: 3544090
On the basis of chemometrics investigation, the design of the mutation of the protein involved as an environment for the catalysis of the asymmetric reaction, transfer hydrogenation, was made. We studied the influence of the amino acid residues to the asymmetric catalysis in order to optimize the catalysts for asymmetric synthesis in the biomimetic environment. This is interesting from scientific as well as commercial point of view. Presented study offered enhanced catalytic activity of optimized systems and showed directions for further improvements.
COBISS.SI-ID: 3516442
The study resulted in important insights on the role of metal (vanadium), which binds to biotin binding site in streptavidin and transforms a nonenzymatic protein into an enantioselective biocatalyst with synthetic utility. The resulting artificial metalloenzyme catalyzes the enantioselective oxidation of prochiral sulfides with good enantioselectivities both for dialkyl and alkyl-aryl substrates (up to 93% enantiomeric excess). The vanadil binding site was determined by the chemoinformatics study (docking) and confirmed experimentally by electron paragmagnetic resonance spectroscopy.
COBISS.SI-ID: 3942938