activity against e coli atcc 25922  (ATCC)


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    Structured Review

    ATCC activity against e coli atcc 25922
    Developing resistance in E. coli <t>ATCC</t> 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.
    Activity Against E Coli Atcc 25922, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance"

    Article Title: Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

    Journal: Microorganisms

    doi: 10.3390/microorganisms8060867

    Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.
    Figure Legend Snippet: Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.

    Techniques Used:

    Peptide 35409-1 effect on  E. coli  membrane. Panels ( a , b ) show  E. coli  ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of  E. coli  ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.
    Figure Legend Snippet: Peptide 35409-1 effect on E. coli membrane. Panels ( a , b ) show E. coli ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of E. coli ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.

    Techniques Used:

    2) Product Images from "Synthesis, biological activities and docking studies of pleuromutilin derivatives with piperazinyl urea linkage"

    Article Title: Synthesis, biological activities and docking studies of pleuromutilin derivatives with piperazinyl urea linkage

    Journal: Journal of Enzyme Inhibition and Medicinal Chemistry

    doi: 10.1080/14756366.2021.1900163

    Time-kill kinetics of compound 6p against MRSA ATCC 33591( a ) and E. coli ATCC 25922 ( b ).
    Figure Legend Snippet: Time-kill kinetics of compound 6p against MRSA ATCC 33591( a ) and E. coli ATCC 25922 ( b ).

    Techniques Used:

    3) Product Images from "Quinoline Antimalarials Increase the Antibacterial Activity of Ampicillin"

    Article Title: Quinoline Antimalarials Increase the Antibacterial Activity of Ampicillin

    Journal: Frontiers in Microbiology

    doi: 10.3389/fmicb.2021.556550

    Plot of inhibition zone diameter against log of chloroquine and quinine concentration in combination with ampicillin (10 μg) using E. coli ATCC 25922 as test organism.
    Figure Legend Snippet: Plot of inhibition zone diameter against log of chloroquine and quinine concentration in combination with ampicillin (10 μg) using E. coli ATCC 25922 as test organism.

    Techniques Used: Inhibition, Concentration Assay

    Checkerboard analysis of drug combinations tested against  E. coli  ATCC 25922. Data presented as a heatmap indicating percent growth inhibition based on OD 595  values. Percent growth reduction values was calculated as 100% – [(OD of treated cells/OD of untreated cells) × 100%] (  Ogundeji et al., 2017 ). Values represent mean values of three replicates.
    Figure Legend Snippet: Checkerboard analysis of drug combinations tested against E. coli ATCC 25922. Data presented as a heatmap indicating percent growth inhibition based on OD 595 values. Percent growth reduction values was calculated as 100% – [(OD of treated cells/OD of untreated cells) × 100%] ( Ogundeji et al., 2017 ). Values represent mean values of three replicates.

    Techniques Used: Inhibition

    Paper strip diffusion test showing  (A,D) , synergism between control antimicrobials trimethoprim (horizontally placed) and sulfamethoxazole (vertically placed);  (B,E)  potentiation of ampicillin strip (horizontal) by quinine (vertical); and  (C,F)  no interaction/slight inhibition between trimethoprim (horizontal) and ampicillin (vertical).  (A–C)  Show interaction against  S. aureus  NCTC 25922 while  (D–F)  shows interaction against  E. coli  ATCC 25922.
    Figure Legend Snippet: Paper strip diffusion test showing (A,D) , synergism between control antimicrobials trimethoprim (horizontally placed) and sulfamethoxazole (vertically placed); (B,E) potentiation of ampicillin strip (horizontal) by quinine (vertical); and (C,F) no interaction/slight inhibition between trimethoprim (horizontal) and ampicillin (vertical). (A–C) Show interaction against S. aureus NCTC 25922 while (D–F) shows interaction against E. coli ATCC 25922.

    Techniques Used: Stripping Membranes, Diffusion-based Assay, Inhibition

    4) Product Images from "Modulation of antimicrobial potency of human cathelicidin peptides against the ESKAPE pathogens and in vivo efficacy in a murine catheter-associated biofilm model"

    Article Title: Modulation of antimicrobial potency of human cathelicidin peptides against the ESKAPE pathogens and in vivo efficacy in a murine catheter-associated biofilm model

    Journal: Biochimica et biophysica acta. Biomembranes

    doi: 10.1016/j.bbamem.2019.07.012

    Disruption of 24 h established biofilm of (A)  S. aureus USA300 and (B)  E. coli  ATCC 25922 by newly designed LL-37 peptides. Determination of the anti-biofilm ability of peptides when compared with daptomycin and rifamycin. The live cell counts in biofilms were determined by XTT assay. A two-tailed unpaired student  t  test was conducted with a p value
    Figure Legend Snippet: Disruption of 24 h established biofilm of (A) S. aureus USA300 and (B) E. coli ATCC 25922 by newly designed LL-37 peptides. Determination of the anti-biofilm ability of peptides when compared with daptomycin and rifamycin. The live cell counts in biofilms were determined by XTT assay. A two-tailed unpaired student t test was conducted with a p value

    Techniques Used: XTT Assay, Two Tailed Test

    5) Product Images from "In Vitro and In Vivo Characterization of NOSO-502, a Novel Inhibitor of Bacterial Translation"

    Article Title: In Vitro and In Vivo Characterization of NOSO-502, a Novel Inhibitor of Bacterial Translation

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01016-18

    Bactericidal activity of NOSO-502 at 4× and 8× MIC against E. coli ATCC 25922 and K. pneumoniae ATCC 43816. Closed circles, drug-free control; closed squares, NOSO-502 at 4× MIC; closed triangles, NOSO-502 at 8× MIC. Experiments were performed in triplicate. Each symbol represents the mean, and error bars indicate the SEMs.
    Figure Legend Snippet: Bactericidal activity of NOSO-502 at 4× and 8× MIC against E. coli ATCC 25922 and K. pneumoniae ATCC 43816. Closed circles, drug-free control; closed squares, NOSO-502 at 4× MIC; closed triangles, NOSO-502 at 8× MIC. Experiments were performed in triplicate. Each symbol represents the mean, and error bars indicate the SEMs.

    Techniques Used: Activity Assay

    6) Product Images from "Lactoferrin Isolation and Hydrolysis from Red Deer (Cervus elaphus) Milk and the Antibacterial Activity of Deer Lactoferrin and Its Hydrolysates"

    Article Title: Lactoferrin Isolation and Hydrolysis from Red Deer (Cervus elaphus) Milk and the Antibacterial Activity of Deer Lactoferrin and Its Hydrolysates

    Journal: Foods

    doi: 10.3390/foods9111711

    Growth curves of E. coli ATCC 25922 incubated with different concentrations of deer Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.
    Figure Legend Snippet: Growth curves of E. coli ATCC 25922 incubated with different concentrations of deer Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.

    Techniques Used: Incubation

    Growth curves of E. coli ATCC 25922 incubated with different concentrations of cow Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.
    Figure Legend Snippet: Growth curves of E. coli ATCC 25922 incubated with different concentrations of cow Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.

    Techniques Used: Incubation

    7) Product Images from "Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin"

    Article Title: Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin

    Journal: Foods

    doi: 10.3390/foods10061305

    Bacterial viability determined using the LIVE / DEAD BacLight TM Bacterial viability kit. Incubation with lactoferricin (Lfcin) and lactoferrampin (Lfampin) at 0 and 24 h. ( A ) E. coli ATCC 25922 incubated with deer Lfcin 240 µg/mL. ( B ) E. coli ATCC 25922 incubated with bovine Lfcin 120 µg/mL. ( C ) E. coli ATCC 25922 incubated with bovine Lfampin 480 µg/mL. ( D ) E. coli ATCC 25922 incubated with penicillin (10,000 units/mL) and streptomycin (10,000 µg/mL). ( E ) E. coli ATCC 25922 incubated with nutrient broth. ( F ) L. acidophilus ATCC4356 incubated with deer Lfcin 480 µg/mL. ( G ) L. acidophilus ATCC4356 incubated with penicillin (10,000 units/mL) and streptomycin (10,000 µg/mL). ( H ) L. acidophilus ATCC4356 incubated with MRSc broth. Green fluorescence indicates viable bacteria, red fluorescence indicates non-viable bacteria. Microscope magnification ×1000.
    Figure Legend Snippet: Bacterial viability determined using the LIVE / DEAD BacLight TM Bacterial viability kit. Incubation with lactoferricin (Lfcin) and lactoferrampin (Lfampin) at 0 and 24 h. ( A ) E. coli ATCC 25922 incubated with deer Lfcin 240 µg/mL. ( B ) E. coli ATCC 25922 incubated with bovine Lfcin 120 µg/mL. ( C ) E. coli ATCC 25922 incubated with bovine Lfampin 480 µg/mL. ( D ) E. coli ATCC 25922 incubated with penicillin (10,000 units/mL) and streptomycin (10,000 µg/mL). ( E ) E. coli ATCC 25922 incubated with nutrient broth. ( F ) L. acidophilus ATCC4356 incubated with deer Lfcin 480 µg/mL. ( G ) L. acidophilus ATCC4356 incubated with penicillin (10,000 units/mL) and streptomycin (10,000 µg/mL). ( H ) L. acidophilus ATCC4356 incubated with MRSc broth. Green fluorescence indicates viable bacteria, red fluorescence indicates non-viable bacteria. Microscope magnification ×1000.

    Techniques Used: Incubation, Fluorescence, Microscopy

    8) Product Images from "Mechanistic Basis for ATP-Dependent Inhibition of Glutamine Synthetase by Tabtoxinine-β-Lactam"

    Article Title: Mechanistic Basis for ATP-Dependent Inhibition of Glutamine Synthetase by Tabtoxinine-β-Lactam

    Journal: Biochemistry

    doi: 10.1021/acs.biochem.7b00838

    TβL-Thr and AAG show L-Gln-dependent bacteriostatic activity towards E. coli ATCC 25922. Panels show growth curves of E. coli ATCC 25922 in chemically defined minimal medium supplemented with ( A ) 2 μM TβL-Thr , ( B ) 100 μM TβL-Thr , and ( C ) 2 μM AAG and variable amounts of L-Gln and L-Glu. Error bars represent standard deviations for three independent trials.
    Figure Legend Snippet: TβL-Thr and AAG show L-Gln-dependent bacteriostatic activity towards E. coli ATCC 25922. Panels show growth curves of E. coli ATCC 25922 in chemically defined minimal medium supplemented with ( A ) 2 μM TβL-Thr , ( B ) 100 μM TβL-Thr , and ( C ) 2 μM AAG and variable amounts of L-Gln and L-Glu. Error bars represent standard deviations for three independent trials.

    Techniques Used: Activity Assay

    9) Product Images from "Rapid and efficient production of cecropin A antibacterial peptide in Escherichia coli by fusion with a self-aggregating protein"

    Article Title: Rapid and efficient production of cecropin A antibacterial peptide in Escherichia coli by fusion with a self-aggregating protein

    Journal: BMC Biotechnology

    doi: 10.1186/s12896-018-0473-7

    MIC assay against E. coli of CeA peptides produced in three different expression systems. Growth inhibition of E. coli ATCC 25922 is shown in the presence of various concentrations of CeA peptide produced in the CF system (white rectangle: CeA-1), AT-HIS system (black rectangle: CeA-2), and SA-ELK16 system (rectangle filled with oblique lines: CeA-3). Chemically synthesized CeA peptide was also tested (rectangle filled with point: CeA). GC, growth control for E. coli ATCC 25922 in the absence of CeA. NC, sterilized Müller–Hinton broth used as the normal control in this experiment. Experiments were performed in triplicate, and standard deviations (error bars) are shown
    Figure Legend Snippet: MIC assay against E. coli of CeA peptides produced in three different expression systems. Growth inhibition of E. coli ATCC 25922 is shown in the presence of various concentrations of CeA peptide produced in the CF system (white rectangle: CeA-1), AT-HIS system (black rectangle: CeA-2), and SA-ELK16 system (rectangle filled with oblique lines: CeA-3). Chemically synthesized CeA peptide was also tested (rectangle filled with point: CeA). GC, growth control for E. coli ATCC 25922 in the absence of CeA. NC, sterilized Müller–Hinton broth used as the normal control in this experiment. Experiments were performed in triplicate, and standard deviations (error bars) are shown

    Techniques Used: Produced, Expressing, Inhibition, Synthesized

    10) Product Images from "Mining Amphibian and Insect Transcriptomes for Antimicrobial Peptide Sequences with rAMPage"

    Article Title: Mining Amphibian and Insect Transcriptomes for Antimicrobial Peptide Sequences with rAMPage

    Journal: Antibiotics

    doi: 10.3390/antibiotics11070952

    Antimicrobial susceptibility and hemolysis test results of seven moderately and highly active putative AMPs. AMPs were tested for their bioactivity against E. coli and S. aureus to determine minimum inhibitory and bactericidal concentrations (MIC and MBC, respectively). AMPs were also tested for their hemolytic activity using pig red blood cells to determine hemolytic concentration (HC 50 ) values. Moderate activity (MIC and MBC in the range of 8–16 μg/mL) and high activity ( ≤ 4 μg/mL) thresholds indicated by the dashed lines. AMPs are ordered by increasing MIC values against E. coli ATCC 25922.
    Figure Legend Snippet: Antimicrobial susceptibility and hemolysis test results of seven moderately and highly active putative AMPs. AMPs were tested for their bioactivity against E. coli and S. aureus to determine minimum inhibitory and bactericidal concentrations (MIC and MBC, respectively). AMPs were also tested for their hemolytic activity using pig red blood cells to determine hemolytic concentration (HC 50 ) values. Moderate activity (MIC and MBC in the range of 8–16 μg/mL) and high activity ( ≤ 4 μg/mL) thresholds indicated by the dashed lines. AMPs are ordered by increasing MIC values against E. coli ATCC 25922.

    Techniques Used: Activity Assay, Concentration Assay

    11) Product Images from "Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance"

    Article Title: Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

    Journal: Microorganisms

    doi: 10.3390/microorganisms8060867

    Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.
    Figure Legend Snippet: Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.

    Techniques Used:

    Peptide 35409-1 effect on  E. coli  membrane. Panels ( a , b ) show  E. coli  ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of  E. coli  ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.
    Figure Legend Snippet: Peptide 35409-1 effect on E. coli membrane. Panels ( a , b ) show E. coli ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of E. coli ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.

    Techniques Used:

    12) Product Images from "Bee Pollen and Bee Bread as a Source of Bacteria Producing Antimicrobials"

    Article Title: Bee Pollen and Bee Bread as a Source of Bacteria Producing Antimicrobials

    Journal: Antibiotics

    doi: 10.3390/antibiotics10060713

    An example of antagonistic interaction between isolated strains (strains 1–21 were isolated from the product BB19, and strains 1 and 2 were derived from the product BB3) and indicatory/reference strains of pathogenic bacteria: ( a )  S. aureus  ATCC 25923, ( b )  S. aureus  ATCC 29213, ( c )  S. epidermidis  ATCC 12228, and ( d )  E. coli  ATCC 25922. Interactions with  P. aeruginosa  ATCC 27853 were a separately analyzed (results not presented).
    Figure Legend Snippet: An example of antagonistic interaction between isolated strains (strains 1–21 were isolated from the product BB19, and strains 1 and 2 were derived from the product BB3) and indicatory/reference strains of pathogenic bacteria: ( a ) S. aureus ATCC 25923, ( b ) S. aureus ATCC 29213, ( c ) S. epidermidis ATCC 12228, and ( d ) E. coli ATCC 25922. Interactions with P. aeruginosa ATCC 27853 were a separately analyzed (results not presented).

    Techniques Used: Isolation, Derivative Assay

    13) Product Images from "Comparative Antimicrobial Activity of Commercial Wound-Care Solutions on Bacterial and Fungal Biofilms"

    Article Title: Comparative Antimicrobial Activity of Commercial Wound-Care Solutions on Bacterial and Fungal Biofilms

    Journal: Annals of plastic surgery

    doi: 10.1097/SAP.0000000000001996

    Effect of Wound Solutions on E. coli. A-C. Biofilms were formed in 100 μl BHI with 1% glucose. E. coli ATCC 25922 (panels A-C) or clinical strains of E. coli (panel D). Organisms were added to tissue culture treated plates and incubated for 24 h at 35°C. After 24 h biofilms were washed with 1X PBS three times and 100 μl 100%, 50% or 25% Vashe (panel A), PhaseOne (panel B) or Mafenide (panel C) were added to the wells. Control wells contained 100 μl 1X PBS. Plates were incubated for 1 m, 10 m, 60 m or 24 h. Wells were washed three times with PBS to remove the wound solutions and reconstituted with 100 μl H 2 O. Bacterial viability was monitored by the CFU assay. D. This data represents the minimum time to kill (CFU=0) clinical strains of E. coli with Vashe, PhaseOne or Mafenide. Bacteria that were not killed at 24 h are indicated by > 24 h. Panels A-D are representative of 3 independent experiments.
    Figure Legend Snippet: Effect of Wound Solutions on E. coli. A-C. Biofilms were formed in 100 μl BHI with 1% glucose. E. coli ATCC 25922 (panels A-C) or clinical strains of E. coli (panel D). Organisms were added to tissue culture treated plates and incubated for 24 h at 35°C. After 24 h biofilms were washed with 1X PBS three times and 100 μl 100%, 50% or 25% Vashe (panel A), PhaseOne (panel B) or Mafenide (panel C) were added to the wells. Control wells contained 100 μl 1X PBS. Plates were incubated for 1 m, 10 m, 60 m or 24 h. Wells were washed three times with PBS to remove the wound solutions and reconstituted with 100 μl H 2 O. Bacterial viability was monitored by the CFU assay. D. This data represents the minimum time to kill (CFU=0) clinical strains of E. coli with Vashe, PhaseOne or Mafenide. Bacteria that were not killed at 24 h are indicated by > 24 h. Panels A-D are representative of 3 independent experiments.

    Techniques Used: Incubation, Colony-forming Unit Assay

    14) Product Images from "Lactoferrin Isolation and Hydrolysis from Red Deer (Cervus elaphus) Milk and the Antibacterial Activity of Deer Lactoferrin and Its Hydrolysates"

    Article Title: Lactoferrin Isolation and Hydrolysis from Red Deer (Cervus elaphus) Milk and the Antibacterial Activity of Deer Lactoferrin and Its Hydrolysates

    Journal: Foods

    doi: 10.3390/foods9111711

    Growth curves of E. coli ATCC 25922 incubated with different concentrations of deer Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.
    Figure Legend Snippet: Growth curves of E. coli ATCC 25922 incubated with different concentrations of deer Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.

    Techniques Used: Incubation

    Growth curves of E. coli ATCC 25922 incubated with different concentrations of cow Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.
    Figure Legend Snippet: Growth curves of E. coli ATCC 25922 incubated with different concentrations of cow Lf and its hydrolysates at 37 °C during a 24-h incubation period. All the curves are the average of triplicate incubations.

    Techniques Used: Incubation

    15) Product Images from "FM-CATH, A Novel Cathelicidin From Fejervarya Multistriata, Shows Therapeutic Potential for Treatment of CLP-Induced Sepsis"

    Article Title: FM-CATH, A Novel Cathelicidin From Fejervarya Multistriata, Shows Therapeutic Potential for Treatment of CLP-Induced Sepsis

    Journal: Frontiers in Pharmacology

    doi: 10.3389/fphar.2021.731056

    Stability detection of FM-CATH. FM-CATH was incubated (A) with different concentrations of NaCl solution at room temperature for 1 h, (B) at the indicated temperatures for 1 h, or (C) with human serum [1:4 (v/v)] at 37°C for the indicated duration before its MICs against E. coli ATCC 25922 were determined. Data are expressed as mean ± SEM (n = 3).
    Figure Legend Snippet: Stability detection of FM-CATH. FM-CATH was incubated (A) with different concentrations of NaCl solution at room temperature for 1 h, (B) at the indicated temperatures for 1 h, or (C) with human serum [1:4 (v/v)] at 37°C for the indicated duration before its MICs against E. coli ATCC 25922 were determined. Data are expressed as mean ± SEM (n = 3).

    Techniques Used: Incubation

    Binding reactions of FM-CATH with LPS and LTA (A) Bacterial agglutination of S. aureus ATCC 25923 (the upper row) and E. coli ATCC 25922 (the lower row), respectively. Bacteria treated with BSA in TBS (a, a’), FM-CATH (25 μM) (b, b’), FM-CATH (25 μM) plus equal volume of 0.2 mg/ ml LPS (c, c’) and 0.2 mg/ ml LTA (d, d’) for 30 min before being stained with Gram staining kit. (B), (C), (D) ITC analysis of FM-CATH binding to LPS, polymyxin B binding to LPS, and FM-CATH binding to LTA, respectively. (E), (F) SPRi analysis of LPS and LTA binding to FM-CATH immobilized on a gold chip, respectively.
    Figure Legend Snippet: Binding reactions of FM-CATH with LPS and LTA (A) Bacterial agglutination of S. aureus ATCC 25923 (the upper row) and E. coli ATCC 25922 (the lower row), respectively. Bacteria treated with BSA in TBS (a, a’), FM-CATH (25 μM) (b, b’), FM-CATH (25 μM) plus equal volume of 0.2 mg/ ml LPS (c, c’) and 0.2 mg/ ml LTA (d, d’) for 30 min before being stained with Gram staining kit. (B), (C), (D) ITC analysis of FM-CATH binding to LPS, polymyxin B binding to LPS, and FM-CATH binding to LTA, respectively. (E), (F) SPRi analysis of LPS and LTA binding to FM-CATH immobilized on a gold chip, respectively.

    Techniques Used: Binding Assay, Agglutination, Staining, Chromatin Immunoprecipitation

    16) Product Images from "In Vitro and In Vivo Characterization of NOSO-502, a Novel Inhibitor of Bacterial Translation"

    Article Title: In Vitro and In Vivo Characterization of NOSO-502, a Novel Inhibitor of Bacterial Translation

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.01016-18

    Bactericidal activity of NOSO-502 at 4× and 8× MIC against E. coli ATCC 25922 and K. pneumoniae ATCC 43816. Closed circles, drug-free control; closed squares, NOSO-502 at 4× MIC; closed triangles, NOSO-502 at 8× MIC. Experiments were performed in triplicate. Each symbol represents the mean, and error bars indicate the SEMs.
    Figure Legend Snippet: Bactericidal activity of NOSO-502 at 4× and 8× MIC against E. coli ATCC 25922 and K. pneumoniae ATCC 43816. Closed circles, drug-free control; closed squares, NOSO-502 at 4× MIC; closed triangles, NOSO-502 at 8× MIC. Experiments were performed in triplicate. Each symbol represents the mean, and error bars indicate the SEMs.

    Techniques Used: Activity Assay

    17) Product Images from "Antimicrobial activities of fungus comb extracts isolated from Indomalayan termite (Macrotermes gilvus Hagen) mound"

    Article Title: Antimicrobial activities of fungus comb extracts isolated from Indomalayan termite (Macrotermes gilvus Hagen) mound

    Journal: AMB Express

    doi: 10.1186/s13568-022-01359-0

    Inhibitory activity of fungus comb extract against  E. coli  ATCC 25922,  P. aeruginosa AT CC 27853 and  S. aureus ATCC  25923 .  A1, B1, C1,  n- hexane extract; A2, B2, C2, ethyl acetate extract; A3, B3, C3, methanol extract; A4, B4,C4, water extract.  a  50 mg;  b  25 mg;  c  2.5 mg; 1, Ampicillin 10 μg; 2, Ciprofloxacin 5 μg; 3, negative control (solvent); 4, fungus comb extracts
    Figure Legend Snippet: Inhibitory activity of fungus comb extract against E. coli ATCC 25922, P. aeruginosa AT CC 27853 and S. aureus ATCC 25923 . A1, B1, C1, n- hexane extract; A2, B2, C2, ethyl acetate extract; A3, B3, C3, methanol extract; A4, B4,C4, water extract. a 50 mg; b 25 mg; c 2.5 mg; 1, Ampicillin 10 μg; 2, Ciprofloxacin 5 μg; 3, negative control (solvent); 4, fungus comb extracts

    Techniques Used: Activity Assay, Negative Control

    18) Product Images from "Rapid Screening of Essential Oils as Substances Which Enhance Antibiotic Activity Using a Modified Well Diffusion Method"

    Article Title: Rapid Screening of Essential Oils as Substances Which Enhance Antibiotic Activity Using a Modified Well Diffusion Method

    Journal: Antibiotics

    doi: 10.3390/antibiotics10040463

    Time-kill curves showing effects of Petitgrain (15) with ( A ) amikacin ( B ) tetracycline and orange (6) with ( C ) amikacin, ( D ) streptomycin, ( E ) tetracycline, and ( F ) chloramphenicol both at 1× MIC against  E. coli  ATCC 25922.
    Figure Legend Snippet: Time-kill curves showing effects of Petitgrain (15) with ( A ) amikacin ( B ) tetracycline and orange (6) with ( C ) amikacin, ( D ) streptomycin, ( E ) tetracycline, and ( F ) chloramphenicol both at 1× MIC against E. coli ATCC 25922.

    Techniques Used:

    19) Product Images from "Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance"

    Article Title: Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

    Journal: Microorganisms

    doi: 10.3390/microorganisms8060867

    Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.
    Figure Legend Snippet: Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.

    Techniques Used:

    Peptide 35409-1 effect on  E. coli  membrane. Panels ( a , b ) show  E. coli  ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of  E. coli  ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.
    Figure Legend Snippet: Peptide 35409-1 effect on E. coli membrane. Panels ( a , b ) show E. coli ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of E. coli ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.

    Techniques Used:

    20) Product Images from "Evaluating Aztreonam and Ceftazidime Pharmacodynamics with Escherichia coli in Combination with Daptomycin, Linezolid, or Vancomycin in an In Vitro Pharmacodynamic Model "

    Article Title: Evaluating Aztreonam and Ceftazidime Pharmacodynamics with Escherichia coli in Combination with Daptomycin, Linezolid, or Vancomycin in an In Vitro Pharmacodynamic Model

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.00180-09

    In vitro activity of linezolid alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b).
    Figure Legend Snippet: In vitro activity of linezolid alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b).

    Techniques Used: In Vitro, Activity Assay

    In vitro activity of daptomycin alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b). Results show log 10 numbers of CFU/ml of activity ± standard deviations.
    Figure Legend Snippet: In vitro activity of daptomycin alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b). Results show log 10 numbers of CFU/ml of activity ± standard deviations.

    Techniques Used: In Vitro, Activity Assay

    In vitro activity of vancomycin alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b).
    Figure Legend Snippet: In vitro activity of vancomycin alone and combined with aztreonam or ceftazidime against E. coli ATCC 25922 (a) and a clinical isolate (b).

    Techniques Used: In Vitro, Activity Assay

    21) Product Images from "Rapid and efficient production of cecropin A antibacterial peptide in Escherichia coli by fusion with a self-aggregating protein"

    Article Title: Rapid and efficient production of cecropin A antibacterial peptide in Escherichia coli by fusion with a self-aggregating protein

    Journal: BMC Biotechnology

    doi: 10.1186/s12896-018-0473-7

    MIC assay against E. coli of CeA peptides produced in three different expression systems. Growth inhibition of E. coli ATCC 25922 is shown in the presence of various concentrations of CeA peptide produced in the CF system (white rectangle: CeA-1), AT-HIS system (black rectangle: CeA-2), and SA-ELK16 system (rectangle filled with oblique lines: CeA-3). Chemically synthesized CeA peptide was also tested (rectangle filled with point: CeA). GC, growth control for E. coli ATCC 25922 in the absence of CeA. NC, sterilized Müller–Hinton broth used as the normal control in this experiment. Experiments were performed in triplicate, and standard deviations (error bars) are shown
    Figure Legend Snippet: MIC assay against E. coli of CeA peptides produced in three different expression systems. Growth inhibition of E. coli ATCC 25922 is shown in the presence of various concentrations of CeA peptide produced in the CF system (white rectangle: CeA-1), AT-HIS system (black rectangle: CeA-2), and SA-ELK16 system (rectangle filled with oblique lines: CeA-3). Chemically synthesized CeA peptide was also tested (rectangle filled with point: CeA). GC, growth control for E. coli ATCC 25922 in the absence of CeA. NC, sterilized Müller–Hinton broth used as the normal control in this experiment. Experiments were performed in triplicate, and standard deviations (error bars) are shown

    Techniques Used: Produced, Expressing, Inhibition, Synthesized

    22) Product Images from "Rapid Screening of Essential Oils as Substances Which Enhance Antibiotic Activity Using a Modified Well Diffusion Method"

    Article Title: Rapid Screening of Essential Oils as Substances Which Enhance Antibiotic Activity Using a Modified Well Diffusion Method

    Journal: Antibiotics

    doi: 10.3390/antibiotics10040463

    Time-kill curves showing effects of Petitgrain (15) with ( A ) amikacin ( B ) tetracycline and orange (6) with ( C ) amikacin, ( D ) streptomycin, ( E ) tetracycline, and ( F ) chloramphenicol both at 1× MIC against  E. coli  ATCC 25922.
    Figure Legend Snippet: Time-kill curves showing effects of Petitgrain (15) with ( A ) amikacin ( B ) tetracycline and orange (6) with ( C ) amikacin, ( D ) streptomycin, ( E ) tetracycline, and ( F ) chloramphenicol both at 1× MIC against E. coli ATCC 25922.

    Techniques Used:

    23) Product Images from "The Influence of Hypericum perforatum L. Addition to Wheat Cookies on Their Antioxidant, Anti-Metabolic Syndrome, and Antimicrobial Properties"

    Article Title: The Influence of Hypericum perforatum L. Addition to Wheat Cookies on Their Antioxidant, Anti-Metabolic Syndrome, and Antimicrobial Properties

    Journal: Foods

    doi: 10.3390/foods10061379

    Viability (in %) of E. coli ATCC 25922 and B. cereus ATCC 14579 against hydrolyzates ( A1 , A2 ) and fractions ( B1 , B2 ) of samples: 0.5 SJW, 1.0 SJW, and control (cookies without St. John’s wort).
    Figure Legend Snippet: Viability (in %) of E. coli ATCC 25922 and B. cereus ATCC 14579 against hydrolyzates ( A1 , A2 ) and fractions ( B1 , B2 ) of samples: 0.5 SJW, 1.0 SJW, and control (cookies without St. John’s wort).

    Techniques Used:

    24) Product Images from "Antimicrobial activities of fungus comb extracts isolated from Indomalayan termite (Macrotermes gilvus Hagen) mound"

    Article Title: Antimicrobial activities of fungus comb extracts isolated from Indomalayan termite (Macrotermes gilvus Hagen) mound

    Journal: AMB Express

    doi: 10.1186/s13568-022-01359-0

    Inhibitory activity of fungus comb extract against  E. coli  ATCC 25922,  P. aeruginosa AT CC 27853 and  S. aureus ATCC  25923 .  A1, B1, C1,  n- hexane extract; A2, B2, C2, ethyl acetate extract; A3, B3, C3, methanol extract; A4, B4,C4, water extract.  a  50 mg;  b  25 mg;  c  2.5 mg; 1, Ampicillin 10 μg; 2, Ciprofloxacin 5 μg; 3, negative control (solvent); 4, fungus comb extracts
    Figure Legend Snippet: Inhibitory activity of fungus comb extract against E. coli ATCC 25922, P. aeruginosa AT CC 27853 and S. aureus ATCC 25923 . A1, B1, C1, n- hexane extract; A2, B2, C2, ethyl acetate extract; A3, B3, C3, methanol extract; A4, B4,C4, water extract. a 50 mg; b 25 mg; c 2.5 mg; 1, Ampicillin 10 μg; 2, Ciprofloxacin 5 μg; 3, negative control (solvent); 4, fungus comb extracts

    Techniques Used: Activity Assay, Negative Control

    25) Product Images from "The Influence of Hypericum perforatum L. Addition to Wheat Cookies on Their Antioxidant, Anti-Metabolic Syndrome, and Antimicrobial Properties"

    Article Title: The Influence of Hypericum perforatum L. Addition to Wheat Cookies on Their Antioxidant, Anti-Metabolic Syndrome, and Antimicrobial Properties

    Journal: Foods

    doi: 10.3390/foods10061379

    Viability (in %) of E. coli ATCC 25922 and B. cereus ATCC 14579 against hydrolyzates ( A1 , A2 ) and fractions ( B1 , B2 ) of samples: 0.5 SJW, 1.0 SJW, and control (cookies without St. John’s wort).
    Figure Legend Snippet: Viability (in %) of E. coli ATCC 25922 and B. cereus ATCC 14579 against hydrolyzates ( A1 , A2 ) and fractions ( B1 , B2 ) of samples: 0.5 SJW, 1.0 SJW, and control (cookies without St. John’s wort).

    Techniques Used:

    26) Product Images from "Comparative Antimicrobial Activity of Commercial Wound-Care Solutions on Bacterial and Fungal Biofilms"

    Article Title: Comparative Antimicrobial Activity of Commercial Wound-Care Solutions on Bacterial and Fungal Biofilms

    Journal: Annals of plastic surgery

    doi: 10.1097/SAP.0000000000001996

    Effect of Wound Solutions on E. coli. A-C. Biofilms were formed in 100 μl BHI with 1% glucose. E. coli ATCC 25922 (panels A-C) or clinical strains of E. coli (panel D). Organisms were added to tissue culture treated plates and incubated for 24 h at 35°C. After 24 h biofilms were washed with 1X PBS three times and 100 μl 100%, 50% or 25% Vashe (panel A), PhaseOne (panel B) or Mafenide (panel C) were added to the wells. Control wells contained 100 μl 1X PBS. Plates were incubated for 1 m, 10 m, 60 m or 24 h. Wells were washed three times with PBS to remove the wound solutions and reconstituted with 100 μl H 2 O. Bacterial viability was monitored by the CFU assay. D. This data represents the minimum time to kill (CFU=0) clinical strains of E. coli with Vashe, PhaseOne or Mafenide. Bacteria that were not killed at 24 h are indicated by > 24 h. Panels A-D are representative of 3 independent experiments.
    Figure Legend Snippet: Effect of Wound Solutions on E. coli. A-C. Biofilms were formed in 100 μl BHI with 1% glucose. E. coli ATCC 25922 (panels A-C) or clinical strains of E. coli (panel D). Organisms were added to tissue culture treated plates and incubated for 24 h at 35°C. After 24 h biofilms were washed with 1X PBS three times and 100 μl 100%, 50% or 25% Vashe (panel A), PhaseOne (panel B) or Mafenide (panel C) were added to the wells. Control wells contained 100 μl 1X PBS. Plates were incubated for 1 m, 10 m, 60 m or 24 h. Wells were washed three times with PBS to remove the wound solutions and reconstituted with 100 μl H 2 O. Bacterial viability was monitored by the CFU assay. D. This data represents the minimum time to kill (CFU=0) clinical strains of E. coli with Vashe, PhaseOne or Mafenide. Bacteria that were not killed at 24 h are indicated by > 24 h. Panels A-D are representative of 3 independent experiments.

    Techniques Used: Incubation, Colony-forming Unit Assay

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    ATCC escherichia coli
    Antibacterial activity of Gly-His dipeptides with or without AgNPs against a) <t>Escherichia</t> <t>coli</t> , b) Staphylococcus aureus , and c) Pseudomonas aeruginosa
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    Antibacterial activity of Gly-His dipeptides with or without AgNPs against a) Escherichia coli , b) Staphylococcus aureus , and c) Pseudomonas aeruginosa

    Journal: Archives of Industrial Hygiene and Toxicology

    Article Title: Antioxidative, Cytotoxic, and Antibacterial Properties of Self-assembled Glycine-histidine-based Dipeptides with or Without Silver Nanoparticles in Bio-inspired Film

    doi: 10.2478/aiht-2022-73-3658

    Figure Lengend Snippet: Antibacterial activity of Gly-His dipeptides with or without AgNPs against a) Escherichia coli , b) Staphylococcus aureus , and c) Pseudomonas aeruginosa

    Article Snippet: The activity of AgNP-decorated Gly-His dipeptide films against Escherichia coli ATCC 25922 (Gram-negative), Staphylococcus aureus ATCC 29213 (Gram-positive), and Pseudomonas aeruginosa ATCC 27853 (Gram-negative) was determined using the disc diffusion method recommended by the European Committee on Antimicrobial Susceptibility Testing (EUCAST) ( ).

    Techniques: Activity Assay

    Inhibition effects of cell-free supernatants against gram-negative bacteria. a: 9PS, b: 25PS, c: 26PS, and d: 27PS against non ESBL-producing E. coli ATCC 25922, while e: 9PS, f: 25PS, g: 26PS, and h: 27PS against ESBL-producing E. coli ATCC 35218.

    Journal: Saudi Journal of Biological Sciences

    Article Title: Screening of Indonesian peat soil bacteria producing antimicrobial compounds

    doi: 10.1016/j.sjbs.2020.05.033

    Figure Lengend Snippet: Inhibition effects of cell-free supernatants against gram-negative bacteria. a: 9PS, b: 25PS, c: 26PS, and d: 27PS against non ESBL-producing E. coli ATCC 25922, while e: 9PS, f: 25PS, g: 26PS, and h: 27PS against ESBL-producing E. coli ATCC 35218.

    Article Snippet: 3.3 Screening of antimicrobial activity The screening tests of antimicrobial activity of all supernatant isolates showed some isolates had no inhibitory effect while others had inhibitory effects against non ESBL-producing E. coli ATCC 25922, ESBL-producing E. coli ATCC 35218, MSSA ATCC 29213, and MRSA ATCC 43300, as indicated by the presence of clear zones around the wells.

    Techniques: Inhibition

    Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.

    Journal: Microorganisms

    Article Title: Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

    doi: 10.3390/microorganisms8060867

    Figure Lengend Snippet: Developing resistance in E. coli ATCC 25922 by 35409-1-treatment. The figure shows MIC variation for bacteria repeatedly treated with 0.5× MIC for peptide 35409-1 compared to MIC variation for bacteria treated with 0.5× MIC for ciprofloxacin and tetracycline.

    Article Snippet: The four derivatives’ (35409-1, -2, -4 and -13) activity against E. coli ATCC 25922 was maintained in the presence of fresh human sera.

    Techniques:

    Peptide 35409-1 effect on  E. coli  membrane. Panels ( a , b ) show  E. coli  ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of  E. coli  ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.

    Journal: Microorganisms

    Article Title: Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

    doi: 10.3390/microorganisms8060867

    Figure Lengend Snippet: Peptide 35409-1 effect on E. coli membrane. Panels ( a , b ) show E. coli ATCC 25922, ( a ) without treatment and ( b ) treated with peptide 35409-1, by SEM. Panel ( c ) shows the permeabilisation of E. coli ML35 Gram-negative membrane evaluated with ONPG. The cecropin P1 peptide was used as positive permeabilisation control as it is recognised for its powerful membrane action. Untreated bacteria and ciprofloxacin-treated bacteria (an antibiotic having intracellular action) were used as negative controls.

    Article Snippet: The four derivatives’ (35409-1, -2, -4 and -13) activity against E. coli ATCC 25922 was maintained in the presence of fresh human sera.

    Techniques:

    Effect of TC NPs  on the viability of a)  B. subtilis  ATCC 6633 and b)  E. coli  ATCC 25922, as monitored by confocal laser scanning microscopy. Representative images of control cultures (top row), and cultures treated with 10 11  TC NPs  (middle and bottom row)

    Journal: Advanced healthcare materials

    Article Title: Destruction of Opportunistic Pathogens via Polymer Nanoparticle-Mediated Release of Plant-Based Antimicrobial Payloads

    doi: 10.1002/adhm.201500974

    Figure Lengend Snippet: Effect of TC NPs on the viability of a) B. subtilis ATCC 6633 and b) E. coli ATCC 25922, as monitored by confocal laser scanning microscopy. Representative images of control cultures (top row), and cultures treated with 10 11 TC NPs (middle and bottom row)

    Article Snippet: Initially, we evaluated the antimicrobial activity of NPs containing pure carvacrol (33% w/w, carvacrol relative to NP) and various ratios of thymol:carvacrol (Treatment I – 66% w/w, 3:1 T:C; Treatment II – 55% w/w, 1.5:1 T:C; and Treatment III – 47% w/w, 0.75:1) against E. coli ATCC 25922, S. aureus RN6390, and B. subtilis ATCC 6633 ( ).

    Techniques: Confocal Laser Scanning Microscopy

    a) TEM of E. coli ATCC 25922 and b) B. subtilis ATCC 6633 control cultures and cultures that were challenged with 10 11 TC NPs for various times. c) High resolution SEM of the control culture of B. subtilis ATCC 6633 and the culture treated for 24 h with

    Journal: Advanced healthcare materials

    Article Title: Destruction of Opportunistic Pathogens via Polymer Nanoparticle-Mediated Release of Plant-Based Antimicrobial Payloads

    doi: 10.1002/adhm.201500974

    Figure Lengend Snippet: a) TEM of E. coli ATCC 25922 and b) B. subtilis ATCC 6633 control cultures and cultures that were challenged with 10 11 TC NPs for various times. c) High resolution SEM of the control culture of B. subtilis ATCC 6633 and the culture treated for 24 h with

    Article Snippet: Initially, we evaluated the antimicrobial activity of NPs containing pure carvacrol (33% w/w, carvacrol relative to NP) and various ratios of thymol:carvacrol (Treatment I – 66% w/w, 3:1 T:C; Treatment II – 55% w/w, 1.5:1 T:C; and Treatment III – 47% w/w, 0.75:1) against E. coli ATCC 25922, S. aureus RN6390, and B. subtilis ATCC 6633 ( ).

    Techniques: Transmission Electron Microscopy

    Evaluation of antimicrobial activity for 10 11  TC NPs  mL–1 on the viability of (●)  E. coli  ATCC 25922, (■)  S. aureus  RN6390, (▲)  B. subtilis  ATCC 6633, (▼)  E. coli  ATCC 43895 (serotype O157:H7), and (◆)  B.

    Journal: Advanced healthcare materials

    Article Title: Destruction of Opportunistic Pathogens via Polymer Nanoparticle-Mediated Release of Plant-Based Antimicrobial Payloads

    doi: 10.1002/adhm.201500974

    Figure Lengend Snippet: Evaluation of antimicrobial activity for 10 11 TC NPs mL–1 on the viability of (●) E. coli ATCC 25922, (■) S. aureus RN6390, (▲) B. subtilis ATCC 6633, (▼) E. coli ATCC 43895 (serotype O157:H7), and (◆) B.

    Article Snippet: Initially, we evaluated the antimicrobial activity of NPs containing pure carvacrol (33% w/w, carvacrol relative to NP) and various ratios of thymol:carvacrol (Treatment I – 66% w/w, 3:1 T:C; Treatment II – 55% w/w, 1.5:1 T:C; and Treatment III – 47% w/w, 0.75:1) against E. coli ATCC 25922, S. aureus RN6390, and B. subtilis ATCC 6633 ( ).

    Techniques: Activity Assay