Oxidative stress, which leads to oxidative modification of various macromolecules, including proteins, is now considered an important pathogenetic link in many diseases. In this work, oxidative damage to a blood plasma protein, bovine serum albumin BSA, under the action of an oxidizing agent, hydrogen peroxide H2O2, was studied by spectrofluorometric method. The H2O2 concentration-dependent quenching of the intrinsic fluorescence of BSA is shown. BSA fluorescence quenching constants in hydrogen peroxide solutions are calculated by mathematical modeling methods. The dependences found in the fluorescence quenching constants are explained both by oxidative damage to the microenvironment of BSA tryptophan residues and by changes in the native conformation of protein globules upon oxidative damage. More significant peroxide damage to BSA occurs at lower pH values due to the fact that H2O2, as an oxidizing agent, acts more strongly in an acidic environment. The registered quenching of the protein's own fluorescence when damaged by an oxidizing agent can be used as a medical method for assessing the level of oxidative stress in the body in the diagnosis of a number of diseases.

Annexin V is an eukaryotic protein from the annexin family which is able to reversibly bind to phospholipid membranes in a Ca²⁺-dependent manner. It possesses a complex mechanism of the membrane binding which includes the two-dimensional lattice formation from annexin V trimers and significant variation of the membrane structure. The precise functions of annexin V are largely unknown, however, its participation in the blood coagulation, membrane repair process and the Ca²⁺ channel activity is suggested. The usage of annexin V as a marker of phosphatidylserine-positive cells in in vitro and in vivo studies makes the understanding of the protein role in cellular processes critically important.

The current review is focused on the structure of annexin V and the mechanism and kinetics of its membrane binding. The lipid specificity and the multimerization process will be described. Finally, some of the proposed annexin V functions including inhibition of the blood coagulation and the Ca²⁺ transport activity will be discussed.

The directed movement of neutrophils is provided by the rapid polymerization of actin with the formation of a protrusion growing forward. In our previous work we observed impaired neutrophil movement for patients with Wiskott-Aldrich syndrome (WAS) compared to healthy donors.

In this work, we set out to explain the impairment of neutrophil chemotaxis in patients by observation and computer modeling of the linear growth rates of the anterior pseudopodia. The neutrophil chemotaxis was observed by means of low-angle fluorescent microscopy in parallel-plate flow chambers. The computational model was constructed as a network-like 2D stochastic polymerization of actin guided by the proximity of cell membrane with branching governed by Arp2/3 and WASP proteins.

The observed linear velocity of neutrophil pseudopodium formation was 0.22 ± 0.04 μm/s for healthy donors and 0.23 ± 0.08 μm/s for WAS patients. The model described the velocity of the pseudopodium formation for healthy donors well. For the description of WAS patients data, a variation of branching velocity (governed by WASP) by an order of magnitude was applied, which did not significantly alter the linear protrusion growth velocity.

We conclude that the proposed mathematical model of neutrophil pseudopodium formation could describe the experimental data well, but the data on overall neutrophil movement could not be explained by the velocities of the pseudopodium growth.

Store-operated calcium entry (SOCE) plays an important role in platelet function. It is generally assumed that the mechanism of SOCE relies on the direct interaction of STIM1 and ORAI1 proteins with specific STIM1:ORAI1 stoichiometry. However, in platelets, other pathways may take place. Here we aim to investigate the mechanisms of SOCE in platelets. We developed a lattice-based mathematical model that represented STIM1-ORAI1 interactions and applied it to both HEK cells, where SOCE mechanism is well established, and platelets. The model was able to describe STIM1-ORAI1 behavior in HEK cells successfully. We used the same parameters for protein interaction and applied them to platelets. As a result, we demonstrated that the number of STIM1 proteins on ER membrane could not assure the needed stoichiometry to proper SOCE in platelets.