scholarly journals Kinetics of Bacterial Inactivation by Peroxynitric Acid in the Presence of Organic Contaminants

2020 ◽  
Vol 87 (2) ◽  
Author(s):  
Takashi Yokoyama ◽  
Shinya Miyazaki ◽  
Hiroko Akagi ◽  
Satoshi Ikawa ◽  
Katsuhisa Kitano
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Bactericidal Activity ◽  
Organic Contaminants ◽  
Biological Fluids ◽  
Bactericidal Effect ◽  
Amino Acid Residues ◽  
Bacterial Inactivation ◽  
Peroxynitric Acid ◽  
Dose Dependent

ABSTRACT Low-temperature atmospheric-pressure plasma has been studied for disinfection purposes. When plasma is exposed to water, reactive oxygen and nitrogen species are generated and preserved in the water fraction (plasma-treated water [PTW]), which consequently exhibits bactericidal activity. At low temperatures, one of the bactericidal components of PTW is peroxynitric acid (PNA). Importantly, PNA can also be synthesized by chemical reaction, without exposure to plasma. In this study, we evaluated the bactericidal properties of PNA based on reaction kinetics in comparison with other disinfectants. The analysis, based on dose-dependent effects, showed that PNA exhibited about 1 and 10 times the bactericidal activity of hypochlorous acid (HOCl) and peracetic acid, respectively. In addition, we evaluated the influence of organic contaminants on the bactericidal effects of PNA and HOCl. The bactericidal potential of both disinfectants was reduced by bovine serum albumin (BSA); however, PNA showed about 30-times-higher resistance against BSA inhibition than HOCl. Analysis of the dose-dependent effects of PNA revealed that the inhibition of bactericidal effect was caused by its consumption. Further experiments using model substrates containing particular amino acid residues (Met, Cys, Lys, and Leu) suggested that the bacterial inactivation by PNA is less affected by BSA due to the low reactivity and narrow reactivity spectrum of PNA for amino acid residues. Overall, our results suggest that PNA has a great disinfection potential, especially in the presence of organic contaminants (e.g., on the surface of the human body and on medical instruments contaminated with biological fluids). IMPORTANCE A good disinfectant for the human body should have various properties, such as strong bactericidal activity, harmlessness to living tissues, and resistance against biological fluids (or other organic contaminants). Peroxynitric acid (PNA) showed a bactericidal effect that was several tens up to several hundred times higher per unit of molarity than that of sodium hypochlorite and peracetic acid, which are used as general disinfectants for medical equipment. Moreover, the high resistance of PNA to organic load was confirmed, indicating that PNA will inactivate bacteria effectively even on contaminated surfaces, such as used medical devices or the human body surface. Therefore, we propose that PNA can be used as a strong disinfectant for the human body.

scholarly journals Susceptibility of Streptococcusmutans and Actinobacillusactinomycetemcomitans to Bactericidal Activity of Human β-Defensin 3 in Biological Fluids

2005 ◽  
Vol 49 (3) ◽  
pp. 1245-1248 ◽  
Author(s):  
Giuseppantonio Maisetta ◽  
Giovanna Batoni ◽  
Semih Esin ◽  
Giorgio Raco ◽  
Daria Bottai ◽  
...  
Keyword(s):  
Bactericidal Activity ◽  
Biological Fluids ◽  
Local Treatment ◽  
Bactericidal Effect ◽  
Therapeutic Use ◽  
Dependent Manner ◽  
Bacterial Strains ◽  
Oral Infections ◽  
Dose Dependent

ABSTRACT Bactericidal activity of human β-defensin 3 (hBD-3) against Streptococcus mutans and Actinobacillus actinomycetemcomitans was inhibited in a dose-dependent manner by the presence of saliva and/or serum. Increasing the concentration of hBD-3 partially overcame this inhibition. A fast bactericidal effect was observed against both bacterial strains, suggesting a potential therapeutic use for hBD-3 in the local treatment of oral infections.

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

scholarly journals Involvement of the N-terminal part of cyclophilin B in the interaction with specific Jurkat T-cell binding sites

1996 ◽  
Vol 317 (2) ◽  
pp. 571-576 ◽  
Author(s):  
Christophe MARILLER ◽  
Bernard HAENDLER ◽  
Fabrice ALLAIN ◽  
Agnès DENYS ◽  
Geneviève SPIK
Keyword(s):  
Amino Acid ◽  
Human Peripheral Blood ◽  
Biological Fluids ◽  
Peripheral Blood Lymphocytes ◽  
Site Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Cyclophilin B ◽  
Jurkat T Cell ◽  
Terminal Amino

Cyclophilin B (CyPB) is secreted in biological fluids such as blood or milk and binds to a specific receptor present on the human lymphoblastic cell line Jurkat and on human peripheral blood lymphocytes. This study was intended to specify the areas of CyPB that are involved in the interaction with the receptor. A synthetic peptide corresponding to the first 24 N-terminal amino acid residues of CyPB was shown to specifically recognize the receptor. Moreover, modification of Arg18 of CyPB by p-hydroxyphenylglyoxal led to a dramatic loss of affinity for the receptor. However, when this residue was replaced by an alanine residue using site-directed mutagenesis, no modification of the binding properties was found, suggesting that Arg18 is not directly involved but is sufficiently close to the interaction site to interfere with the binding when modified. Competitive binding experiments using a chimaeric protein made up of the 24 N-terminal amino acid residues of CyPB fused to the cyclophilin A core sequence confirmed the involvement of this region of CyPB in receptor binding.

scholarly journals Estimation of the selectivity of sorbents for IgG binding based on tripeptide ligands

2021 ◽  
Vol 65 (3) ◽  
pp. 303-308
Author(s):  
Y. S. Pustsyulga ◽  
O. V. Gribovskaya ◽  
E. M. Ermola ◽  
V. P. Golubovich ◽  
A. G. Moiseenok
Keyword(s):  
Amino Acid ◽  
Plasma Protein ◽  
Aromatic Amino Acid ◽  
Plasma Proteins ◽  
Biological Fluids ◽  
Amino Acid Residues ◽  
Total Plasma ◽  
Igg Binding ◽  
Total Plasma Protein ◽  
Low Activity

Biospecific sorbents for the removal of IgG and subclasses from biological fluids based on oligopeptides, containing aromatic amino acid residues, were created. The selectivity properties of specific sorbents for IgM, IgE, and plasma proteins were evaluated. It was found that the created sorbents exhibit the low activity to the total plasma protein, albumin, IgM, IgE and are highly specific for IgG.

scholarly journals Identification and characteristics of a novel cecropin from the armyworm, Mythimna separata

2020 ◽  
Author(s):  
Kaiqi Lian ◽  
Mingliang Zhang ◽  
Xiuli Liang ◽  
Lingling Zhou ◽  
Zhiqi Shi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Membrane Damage ◽  
Bactericidal Effect ◽  
Klebsiella Pneumonia ◽  
Amino Acid Residues ◽  
Mythimna Separata ◽  
Cell Membrane Damage ◽  
E Coli ◽  
Recent Emergence

Abstract Background: The recent emergence of antibiotic-resistant strains of bacteria has increased the need to develop effective alternatives to antibiotics. Antimicrobial peptides have been considered as a promising product with several advantages.Results: In this present study, we identified a novel cecropin from the armyworm, Mythimna separata (armyworm cecropin 1, AC-1) by transcriptome sequencing and multi-sequence alignment analysis. The AC-1 precursor comprised 63 amino acid residues, containing a conserved cleavage site of the signal peptide, Ala23-Pro24, while the mature AC-1 included 39 amino acid residues. Chemically synthesized AC-1 exhibited low hemolytic activity against chicken red blood cells, low cytotoxicity against swine testis cells, and effective antimicrobial activity against Salmonella, Escherichia coli, Klebsiella pneumonia, and Pseudomonas aeruginosa. Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100 °C or in 250 mM NaCl, KCl, or MgCl2 solution, implying good thermal- and salt-resistant stabilities. The bactericidal effect of AC-1 on E. coli gradually increased with increasing AC-1 concentration, resulting in deformation, severe edema, cytolysis, cell membrane damage, and reducing intracellular electron density. Additionally, recombinant AC-1 protein expressed in E. coli was digested by enterokinase protease to obtain AC-1, which showed similar antimicrobial activity against E. coli to chemically synthesized AC-1.Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

scholarly journals Identification and characteristics of a novel cecropin from the armyworm, Mythimna separata

2020 ◽  
Author(s):  
Kaiqi Lian ◽  
Mingliang Zhang ◽  
Xiuli Liang ◽  
Lingling Zhou ◽  
Zhiqi Shi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Membrane Damage ◽  
Bactericidal Effect ◽  
Klebsiella Pneumonia ◽  
Amino Acid Residues ◽  
Mythimna Separata ◽  
Cell Membrane Damage ◽  
E Coli ◽  
Recent Emergence

Abstract Background: The recent emergence of antibiotic-resistant strains of bacteria has increased the need to develop effective alternatives to antibiotics. Antimicrobial peptides have been considered as a promising product with several advantages.Results: In this present study, we identified a novel cecropin from the armyworm, Mythimna separata (armyworm cecropin 1, AC-1) by transcriptome sequencing and multi-sequence alignment analysis. The AC-1 precursor comprised 63 amino acid residues, containing a conserved cleavage site of the signal peptide, Ala23-Pro24, while the mature AC-1 included 39 amino acid residues. Chemically synthesized AC-1 exhibited low hemolytic activity against chicken red blood cells, low cytotoxicity against swine testis cells, and effective antimicrobial activity against Salmonella, Escherichia coli, Klebsiella pneumonia, and Pseudomonas aeruginosa. Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100 °C or in 250 mM NaCl, KCl, or MgCl2 solution, implying good thermal- and salt-resistant stabilities. The bactericidal effect of AC-1 on E. coli gradually increased with increasing AC-1 concentration, resulting in deformation, severe edema, cytolysis, cell membrane damage, and reducing intracellular electron density. Additionally, recombinant AC-1 protein expressed in E. coli was digested by enterokinase protease to obtain AC-1, which showed similar antimicrobial activity against E. coli to chemically synthesized AC-1.Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

scholarly journals Macedocin, a Food-Grade Lantibiotic Produced by Streptococcus macedonicus ACA-DC 198

2002 ◽  
Vol 68 (12) ◽  
pp. 5891-5903 ◽  
Author(s):  
Marina D. Georgalaki ◽  
Erika Van den Berghe ◽  
Dimitrios Kritikos ◽  
Bart Devreese ◽  
Jozef Van Beeumen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Pathogenic Bacteria ◽  
Electrospray Mass Spectrometry ◽  
Proteolytic Enzymes ◽  
Bactericidal Effect ◽  
Indicator Strain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Producer Strain ◽  
Food Grade

ABSTRACT Streptococcus macedonicus ACA-DC 198, a strain isolated from Greek Kasseri cheese, produces a food-grade lantibiotic named macedocin. Macedocin has a molecular mass of 2,794.76 ± 0.42 Da, as determined by electrospray mass spectrometry. Partial N-terminal sequence analysis revealed 22 amino acid residues that correspond with the amino acid sequence of the lantibiotics SA-FF22 and SA-M49, both of which were isolated from the pathogen Streptococcus pyogenes. Macedocin inhibits a broad spectrum of lactic acid bacteria, as well as several food spoilage and pathogenic bacteria, including Clostridium tyrobutyricum. It displays a bactericidal effect towards the most sensitive indicator strain, Lactobacillus sakei subsp. sakei LMG 13558T, while the producer strain itself displays autoinhibition when it is grown under conditions that do not favor bacteriocin production. Macedocin is active at pHs between 4.0 and 9.0, and it retains activity even after incubation for 20 min at 121°C with 1 atm of overpressure. Inhibition of macedocin by proteolytic enzymes is variable.

scholarly journals Bactericidal Activity of Increasing Daily and Weekly Doses of Moxifloxacin in Murine Tuberculosis

2002 ◽  
Vol 46 (6) ◽  
pp. 1875-1879 ◽  
Author(s):  
Tetsuyuki Yoshimatsu ◽  
Eric Nuermberger ◽  
Sandeep Tyagi ◽  
Richard Chaisson ◽  
William Bishai ◽  
...  
Keyword(s):  
Bactericidal Activity ◽  
Pharmacokinetic Profile ◽  
Bactericidal Effect ◽  
In Vivo Studies ◽  
Pharmacokinetic Data ◽  
Time Curve ◽  
Pharmacodynamic Profile ◽  
Days Of Therapy ◽  
Dose Dependent

ABSTRACT Moxifloxacin (MXF) is a new 8-methoxyquinolone with potent activity against Mycobacterium tuberculosis and a half-life of 9 to 12 h in humans. Previous in vivo studies using daily doses of 100 mg/kg of body weight have demonstrated bactericidal activity comparable to that of isoniazid (INH) in a murine model of tuberculosis (TB). Recent pharmacokinetic data suggest that MXF may have been underadministered in these studies and that a 400-mg/kg dose in mice better approximates the area under the concentration-time curve obtained in humans after a 400-mg oral dose. Therefore, the bactericidal activity of MXF in doses up to 400 mg/kg given daily or weekly for 28 days was assessed in mice infected intravenously with 5 × 106 CFU of M. tuberculosis. INH was used as a positive control. After 3 days of daily therapy, the CFU counts from splenic homogenates for mice treated with MXF in doses of 100 to 400 mg/kg/day were lower than those from pretreatment controls. No significant differences in CFU counts were seen when mice receiving INH or MXF at 50 mg/kg/day were compared to pretreatment controls. After 28 days of therapy, dose-dependent reductions in CFU counts in splenic homogenates were seen for daily MXF therapy. The maximum bactericidal effect was seen with daily doses of 400 mg/kg, which resulted in a reduction in CFU counts of 1 log10 greater than that with INH treatment, although the difference was not statistically significant. CFU counts from lung homogenates after 28 days of therapy were significantly lower in all treatment groups than in untreated controls. The weekly administration of MXF in doses ranging from 50 to 400 mg/kg resulted in no significant bactericidal activity. Mice receiving daily MXF doses of 200 and 400 mg/kg/day failed to gain weight and appeared ill after 28 days of therapy, findings suggestive of drug toxicity. In conclusion, MXF has dose-dependent bactericidal activity against M. tuberculosis in the mouse when given in doses up to 400 mg/kg, where its pharmacokinetic profile better approximates that of standard human dosages. Combination regimens which take advantage of the enhanced pharmacodynamic profile of MXF at these doses have the potential to shorten the course of antituberculous therapy or allow more intermittent (i.e., once-weekly) therapy and should be evaluated in the mouse model of TB.

scholarly journals Identification and characteristics of a novel cecropin from the armyworm, Mythimna separata

2020 ◽  
Author(s):  
Kaiqi Lian ◽  
Mingliang Zhang ◽  
Xiuli Liang ◽  
Lingling Zhou ◽  
Zhiqi Shi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Membrane Damage ◽  
Bactericidal Effect ◽  
Klebsiella Pneumonia ◽  
Amino Acid Residues ◽  
Mythimna Separata ◽  
Cell Membrane Damage ◽  
Recent Emergence ◽  
Low Cytotoxicity

Abstract Background: The recent emergence of antibiotic-resistant strains of bacteria has increased the need to develop effective alternatives to antibiotics. Antimicrobial peptides have been considered as a promising product with several advantages. Results: In this present study, we identified a novel cecropin from the armyworm, Mythimna separata (armyworm cecropin 1, AC-1) by transcriptome sequencing and multi-sequence alignment analysis . The AC-1 precursor comprised 63 amino acid residues, containing a conserved cleavage site of the signal peptide, Ala 23 -Pro 24 , while the mature AC-1 included 39 amino acid residues. Chemically-synthesized AC-1 exhibited low hemolytic activity against chicken red blood cells, low cytotoxicity against swine testis cells, and effective antimicrobial activity against Salmonella , Escherichia coli ( E. c oli ), Klebsiella pneumonia ( K. pneumonia ), and Pseudomonas aeruginosa ( P . aeruginosa ). Its antimicrobial activity against Salmonella remained after incubation for 1 h at 100 °C or in 250 mM NaCl, KCl, and MgCl 2 solution, implying good thermal- and salt-resistant stabilities. The bactericidal effect of AC-1 on E. c oli gradually increased with the increase of AC-1 concentration, and AC-1 could cause significant deformation , severe edema, cytoplasmic lysis, cell membrane damage of E. c oli , and reduce intracellular electron density. Additionally, the fusion protein AC-1 expressed in E. coli was digested by enterokinase protease to obtain the AC-1, which showed similar antimicrobial activity against E. c oli with chemically-synthesized AC-1. Conclusions: This study identified a novel antimicrobial peptide that may represent a potential alternative to antibiotics.

A FACTOR VIII BINDING DOMAIN RESIDES WITHIN THE AMINO-TERMINAL 272 AMINO ACID RESIDUES OF VON WILLEBRAND FACTOR

1987 ◽  
Author(s):  
P A Foster ◽  
C A Fulcher ◽  
T Marti ◽  
K Titani ◽  
T S Zimmerman
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Factor Viii ◽  
Von Willebrand Factor ◽  
Dependent Manner ◽  
Amino Acid Residues ◽  
Amino Terminal ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Dose Dependent

We have identified a Factor VIII (FVIII) binding domain residing within the amino-terminal 272 amino acid residues of the mature von Willebrand Factor (vWF) subunit. Two dimensional crossed immunoelectrophoresis showed direct binding of purified human FVIII to purified human vWF. After proteolytic digestion of vWF with Staphylococcus aureus V8 protease, FVIII binding was seen only with the amino-terminal SP fragment III and not with the carboxy-terminal SP fragment II. A monoclonal anti-vWF antibody (C3) partially blocked FVIII binding to vWF and SP fragment III. FVIII also bound to vWF which had been adsorbed to polystyrene beads. This binding was inhibited in a dose dependent manner by whole vWF, SP fragment III, and by monoclonal antibody C3. Binding could not be inhibited by SP fragment I, which contains the middle portion of the vWF molecule, or by reduced and alkylated whole vWF. SP fragment II caused only minor inhibition. Trypsin cleavage of SP fragment III produced a 35-kDa fragment containing the amino-terminal 272 amino acid residues of vWF. This fragment reacted with monoclonal antibody C3 and inhibited the binding of FVIII to vWF in a dose dependent manner. The other major fragment obtained from this digestion was a two chain hetero-dimer composed of amino acid residues 273-511 and 674-728. This fragment did not inhibit FVIII binding. These studies demonstrate that a major FVIII binding site resides within the first 272 amino acid residues of vWF.

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