Publications by authors named "Alexander V Michailov"

The interactions of DNA with lysozyme in the surface layer were studied by performing infrared reflection-absorption spectroscopy (IRRAS), ellipsometry, surface tensiometry, surface dilational rheology, and atomic force microscopy (AFM). A concentrated DNA solution was injected into an aqueous subphase underneath a spread lysozyme layer. While the optical properties of the surface layer changed fast after DNA injection, the dynamic dilational surface elasticity almost did not change, thereby indicating no continuous network formation of DNA/lysozyme complexes, unlike the case of DNA interactions with a monolayer of a cationic synthetic polyelectrolyte.

View Article and Find Full Text PDF

The spread layers of lysozyme (LYS) microgel particles were studied by surface dilational rheology, infrared reflection-absorption spectra, Brewster angle microscopy, atomic force microscopy, and scanning electron microscopy. It is shown that the properties of LYS microgel layers differ significantly from those of ß-lactoglobulin (BLG) microgel layers. In the latter case, the spread protein layer is mainly a monolayer, and the interactions between particles lead to the increase in the dynamic surface elasticity by up to 140 mN/m.

View Article and Find Full Text PDF

The formation of ordered 2D nanostructures of double stranded DNA molecules at various interfaces attracts more and more focus in medical and engineering research, but the underlying intermolecular interactions still require elucidation. Recently, it has been revealed that mixtures of DNA with a series of hydrophobic cationic polyelectrolytes including poly(,-diallyl--hexyl--methylammonium) chloride (PDAHMAC) form a network of ribbonlike or threadlike aggregates at the solution-air interface. In the present work, we adopt a novel approach to confine the same polyelectrolyte at the solution-air interface by spreading it on a subphase with elevated ionic strength.

View Article and Find Full Text PDF
Article Synopsis
  • The addition of denaturants significantly alters the surface properties of aqueous myoglobin solutions, differentiating them from mixed solutions of other globular proteins like BSA, lysozyme, and BLG.
  • Dynamic surface elasticity studies reveal that myoglobin solutions with guanidine hydrochloride (GuHCl) exhibit a rapid increase in elasticity followed by a slower rise, potentially due to protein aggregation at the surface, contrasting with the behavior seen in other globular proteins.
  • Ionic surfactants form complexes with myoglobin, leading to unique multistep adsorption kinetics that differ from the interactions observed with other proteins, as confirmed by advanced techniques like ellipsometry and infrared spectroscopy.
View Article and Find Full Text PDF

The adsorption layers of complexes between DNA and oppositely charged surfactants dodecyltrimethylammonium bromide (DTAB) and cetyltrimethylammonium bromide (CTAB) at the solution/air interface were studied with surface tensiometry, dilational surface rheology, atomic force microscopy, Brewster angle microscopy, infrared absorption-reflection spectroscopy, and ellipsometry. Measurements of the kinetic dependencies of the surface properties gave a possibility to discover the time intervals corresponding to the coexistence of two-dimensional phases. One can assume that the observed phase transition is of the first order, unlike the formation of microaggregates in the adsorption layers of mixed solutions of synthetic polyelectrolytes and surfactants.

View Article and Find Full Text PDF