The Properties of Activated Carbons Functionalized with an Antibacterial Agent and a New SufA Protease Inhibitor.

is the cause of many diseases, including numerous infections of the skin. One way to help combat skin infections is to use bandages containing activated carbon. Currently, there are no dressings on the market that use the synergistic effect of activated carbon and antibiotics.

Antibacterial Agents Adsorbed on Active Carbon: A New Approach for and Pathogen Elimination.

Antibiotic overuse and mass production have led to a global problem with the treatment of antibacterial infections. Thus, any possibility to limit the number of antibacterial drugs used will contribute to a decrease in the development of pathogenic bacterial resistance. In this study, the enhanced bacterial growth reduction of pharmaceutical activated carbon (PAC) material with adsorbed antimicrobial agents compared to the activity of pure antibacterial drugs was investigated.

A rapid method for protein staining in polyacrylamide gels using water saturated with chloroform.

Polyacrylamide gel electrophoresis, followed by an appropriate staining, is a popular and useful analytical procedure for protein identification and characterization. The aim of this study was to develop a method for protein visualization in polyacrylamide gels that would be alternative to Coomassie blue or silver staining. The proposed method is simple, fast and inexpensive.

Determination of mechanisms of action of active carbons as a feed additive.

Activated carbon's porous structure allows it to adsorb a substrates, products and catalysts from the environment thus modificated the biocatalysis processes in digestive tract. Active carbons are currently used to remove solvents from gas streams and for water purification; however, few studies have examined the mechanisms of action of active carbon during the biotransformation processes in the digestive tracks. The potential benefits of using activated carbon in feed are uncertain because both its chemical and physical properties can vary significantly depending on the type of carbonaceous feedstock.

New diaryl ω-(isothiocyanato)alkylphosphonates and their mercapturic acids as potential antibacterial agents.

Thirty-four novel, diaryl ω-(isothiocyanato)alkylphosphonates with chlorine atom and methoxy, dimethoxy, methylsulfanyl, or methoxycarbonyl groups at ortho, meta, or para positions of the phenyl ring, and with an unbranched alkyl chain (n = 2-6) were designed and synthesized in a one-pot reaction in 11-76% yields. All isothiocyanates thus generated were evaluated for the first time for antibacterial activity on Pseudomonas aeruginosa and Staphylococcus aureus bacterial strains, and had satisfactory antibacterial activity in most cases. The highest activity, similar to that of reference gentamicin activity against S.

The Lord of the Bacteria: The Fellowship of the Leader and Other Serine Protease Inhibitors.

Since antibiotics use is currently limited due to undesired side effects and the increasing antibiotic resistance of various bacteria strains, there is a pressing need to develop new strategies and methods preventing epidemic outbreaks. The virulent potency of bacteria relies on a number of different extracellularly secreted factors among which proteases considered as promising, novel drug targets are of special interest. The first evidence that bacterial cysteine, serine and metalloproteinases contributed to the progression of infection was found in the early 70's.

The role of serine proteases in the pathogenesis of bacterial infections.

An increasing resistance of pathogenic bacterial species has been considered as one of the major health problems worldwide. The discovery of novel protein targets and development of effective anti-bacterial therapeutics is of high need since for some extremely resistant pathogens we are simply left unarmed. One of new promising therapeutic strategy is the application of specific inhibitors targeting bacterial serine proteases.

Synthesis of novel phosphonic-type activity-based probes for neutrophil serine proteases and their application in spleen lysates of different organisms.

Neutrophils are a type of granulocyte important in the "first line of defense" of the innate immune system. Upon activation, they facilitate the destruction of invading microorganisms by the production of superoxide radicals, as well as the release of the enzymatic contents of their lysozymes. These enzymes include specific serine proteases: cathepsin G, neutrophil elastase, proteinase 3, as well as the recently discovered neutrophil serine protease 4 (NSP4).

Determination of cathepsin G in endometrial tissue using a surface plasmon resonance imaging biosensor with tailored phosphonic inhibitor.

Objective: Cathepsin G is a serine peptidase whose physiological role is mainly associated with an early immune response, anti-microbial activity as well as platelet activation or hydrolysis of coagulation factors. In addition, since the activity of cathepsin G has been associated with the development of various pathological disorders, the measurement of its activity in patient samples is of high interest. Unfortunately, the usefulness of common immunological methods is limited, since they cannot distinguish between catalytically active and inactive protease.

Substrate profiling of Finegoldia magna SufA protease, inhibitor screening and application to prevent human fibrinogen degradation and bacteria growth in vitro.

SufA, which belongs to the subtilisin-like serine protease family, contains a non-canonical Asp-His-Ser catalytic triad. Under in vitro conditions, SufA is capable of human fibrinogen hydrolysis leading to inhibition of fibrin network formation, thus suggesting its important role in the development and progression of Finegoldia magna infections. In addition, it has been demonstrated that SufA can hydrolyze antibacterial peptides such as LL-37 and the chemokine MIG/CXCL 9, hence evading host defence mechanisms.

Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus.

Staphylococcus aureus is responsible for a variety of human infections, including life-threatening, systemic conditions. Secreted proteome, including a range of proteases, constitutes the major virulence factor of the bacterium. However, the functions of individual enzymes, in particular SplA protease, remain poorly characterized.

Phosphonic analogues of glutamic acid as irreversible inhibitors of Staphylococcus aureus endoproteinase GluC: an efficient synthesis and inhibition of the human IgG degradation.

Endoproteinase GluC (V8 protease) is one of many virulence factors released by the Staphylococcus aureus species in vivo. The V8 protease is able to hydrolyze some serpins and all classes of mammalian immunoglobulins. The application of specific and potent inhibitors of V8 protease may lead to the development of new antibacterial agents.

The development of first Staphylococcus aureus SplB protease inhibitors: phosphonic analogues of glutamine.

Produced by Staphylococcus aureus, SplB belongs to the chymotrypsin-like serine protease family. Since the biological role of SplB protease is unknown, the design and application of its specific inhibitors may help to reveal the function of this enzyme. Until now no SplB inhibitors have been reported.