Diamond nanoparticles (NDs) have demonstrated great promise as useful materials in a variety of biomedical settings. In this paper, the antimicrobial and antibiofilm activities of variously functionalized NDs against two common bacterial targets Gram‐negative bacterium Escherichia coli and Gram‐positive bacterium Staphylococcus aureus are compared. Hydroxylated (ND‐OH), aminated (ND‐NH2), carboxylated (ND‐COOH), mannose (ND‐Mannose), tri‐thiomannoside (ND‐Man3), or tri‐thiolactoside (ND‐Lac3)‐modified NDs are fabricated and evaluated in the present work. Of these, the mannose‐modified NDs are found to interfere most strongly with the survival of S. aureus, but not to influence the growth of E. coli. In contrast, particles featuring lactosyl units have the opposite effect on S. aureus growth. Sugar‐functionalized NPs reported to display antibacterial effects are rare. Only ND‐COOH particles are seen to have any effect on the growth profile of E. coli, but the effects are moderate. On the other hand, both ND‐NH2 and ND‐COOH are found to inhibit E. coli‐induced biofilm formation at levels comparable to the known E. coli biofilm disruptor, ampicillin (albeit at concentrations of 100 μg mL−1). However, none of the modified particles examined here reveal any significant activity as disruptors of S. aureus‐induced biofilm formation even at the highest concentrations studied.

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Peptidase of Bacillus thuringiensis var. israelensis IМV В-7465 was isolated from culture supernatant using consecutive fractionations by an ammonium sulphate (60% saturation), ion-exchange chromatography and gel-filtration on the TSK-gels Toyoperl HW-55 and DEAE 650(M). Specific elastase (442 U∙mg of protein-1) and collagenase (212.7 U∙mg of protein-1) activities of the purified enzyme preparation were 8.0- and 6.1-fold, respectively higher than ones of the culture supernatant. Peptidase yields were 33.5% for elastase activity and 30.1% for collagenase activity. It was established that the enzyme is serine metal-dependent alkaline peptidase with Mr about 37 kDa. Maximal hydrolysis of elastin and collagen occurs at the optimum pH 8.0 and t° – 40 and 50 °С, respectively. The purified preparation has high stability at pH in the range of 7.0 to 10.0 and 40-50 °С.

AimTo purify the platelet aggregation inhibitor from Echis multisquamatis snake venom (PAIEM) and characterize its effect on platelet aggregation and HeLa cell proliferation.MethodsSodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) were used for PAIEM identification. Platelet aggregation in the presence of PAIEM was studied on aggregometer Solar-AP2110. The changes of shape and granularity of platelets in the presence of PAIEM were studied on flow cytometer COULTER EPICS XL, and degranulation of platelets was estimated using spectrofluorimetry. Indirect enzyme-linked immunosorbent assay was used for the determination of target of PAIEM on platelet surface. An assay based on 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide was used to evaluate the effect of PAIEM on the proliferation of HeLa cells in cell culture.ResultsThe molecular weight of the protein purified from Echis multisquamatis venom was 14.9 kDa. Half-maximal inhibitory concentration (IC50) of PAIEM needed to inhibit adenosine diphosphate (ADP)-induced platelet aggregation was 7 μM. PAIEM did not affect thrombin- or ADP-induced platelet activation, but it did prevent binding of the anti-IIb antibody to glycoprotein IIb/IIIa (GPIIbIIIa)-receptor of adhered platelets and inhibited the viability of HeLa cells by 54%.ConclusionAs a member of the disintegrin family, PAIEM inhibited platelet aggregation and cell proliferation possibly by blocking integrin-mediated interactions. However, it did not impair cellular signaling causing any changes in platelet shape and granularity and did not affect ADP-induced platelet degranulation. This disintegrin was shown to be a potent inhibitor of integrin-mediated cellular interactions including platelet aggregation or cancer cell proliferation.