Publications by authors named "Igor Yamskov"

The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of conformational thermal transition (65 °C) was determined, after which the peptide-protein complex passes into a denatured stable state.

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For biomedical applications, chitosan and oligochitosan must be appropriately characterized and meet pharmacological requirements in terms of contamination by residual heavy metals. In this work, a series of commercial chitosans was analyzed by ICP-MS method, and high concentration of Fe (44-382 ppm), Cr (3.1-35.

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It is well known that chitosan degradation by nitrous acid leads to oligochitosan (oligoCHI-ahm) bearing reactive 2,5-anhydromannose (3,4-dihydroxy-5-hydroxymethyl-tetrahydrofuran-2-aldehyde) units at the new reducing ends of macromolecules. Standard protocol requires reduction of oligoCHI-ahm with NaBH to corresponding oligoCHI-hml bearing unreactive hydroxymethyl group instead of reactive aldehyde group. For the first time, HP SEC as well as UV and CD spectroscopy methods have revealed that the reduction leads to an indefinite side modification and the formation of a branched oligoCHI-hml with increased molecular weight.

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Article Synopsis
  • Light scattering studies show that oligochitosan solutions have aggregates below a certain pH, while a gel phase appears at or above this critical pH.
  • The presence of D-glucosamine raises the critical pH and enhances the antibacterial effectiveness of oligochitosan against several bacterial strains in neutral and slightly alkaline conditions.
  • Findings suggest that the antimicrobial properties of oligochitosan are linked to its individual molecular structure rather than its larger aggregates, indicating potential for biomedical applications.
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Silver nanoparticles were prepared by reduction of the corresponding metal salt with NaBH(4) in the presence of appropriate dispersing agents, namely, copolymers of maleic acid: poly(N-vinyl-2-pyrrolidone-alt-maleic acid), poly(ethylene-alt-maleic acid), poly(styrene-alt-maleic acid) or their amphyphilic derivatives. A thorough study of the whole process of silver nanoparticles production including formation of polymeric silver salt and stabilization of nanoparticles has been carried out. The degree of cooperativity of copolymer silver ions binding process and binding capacity of copolymers with respect to silver ions was calculated.

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The modification of hydrophobic polyethylene/polystyrene surfaces of medical devices with bilayer/multilayer coatings (BCs/MCs) based on polyelectrolyte complexes (PEC) of modified poly(N-vinylpyrrolidone-co-maleic acid) copolymer (VPMA) with chitosan, amphiphilic chitosan, or albumin was studied. The VPMA contained l-Lysine as affinity ligand for plasminogen attached through alpha-amino group. The surface properties and chemical composition of the surfaces investigated were analyzed, using sessile-drop water contact angle measurements, attenuated total reflectance Fourier-transform infrared spectroscopy (ATR-FTIR), X-ray photoelectron spectroscopy (XPS), and atomic force microscopy (AFM).

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To shed light on the mechanism of isotopic exchange of alpha-protons in amino acids catalyzed by pyridoxal phosphate (PLP)-dependent enzymes, we studied the kinetics of quinonoid intermediate formation for the reactions of tyrosine phenol-lyase with L-phenylalanine, L-methionine, and their alpha-deuterated analogues in D2O, and we compared the results with the rates of the isotopic exchange under the same conditions. We have found that, in the L-phenylalanine reaction, the internal return of the alpha-proton is operative, and allowing for its effect, the exchange rate is accounted for satisfactorily. Surprisingly, for the reaction with L-methionine, the enzymatic isotope exchange went much faster than might be predicted from the kinetic data for quinonoid intermediate formation.

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The principle of affinity chromatography was used for preparation of thromboresistant bilayer coatings. The outer biospecific layer containing epsilon-aminocaproic acid residues (from 2.2 up to 5.

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