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ib m antibacterial peptides against e coli atcc 25922  (ATCC)


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    Structured Review

    ATCC ib m antibacterial peptides against e coli atcc 25922
    (A-C) <t>E.</t> <t>coli</t> without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.
    Ib M Antibacterial Peptides Against E Coli Atcc 25922, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 52584 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibacterial+peptide/Escherichia+coli+(Migula)+Castellani+and+Chalmers/pmc12507217-411-10-16
    Average 99 stars, based on 52584 article reviews
    ib m antibacterial peptides against e coli atcc 25922 - by Bioz Stars, 2026-09
    99/100 stars

    Images

    1) Product Images from "Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides"

    Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

    Journal: PLOS One

    doi: 10.1371/journal.pone.0334029

    (A-C) E. coli without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.
    Figure Legend Snippet: (A-C) E. coli without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.

    Techniques Used:

    (A, F) E. coli without treatment. (B, G) Ib-M1. ( C, H, and I ) Ib-M2. (D, J) Ib-M6. (E, K) E. coli treated with PMB. The alterations are indicated as follows: cytoplasmic retraction (black bracket), bulges (white arrowhead), invagination (yellow arrow), electron-dense material (black arrow and arrowhead), lysed cells (black oval), cytoplasmic vacuoles (thin black arrow), cellular debris-lipid material (black square), and pore (white arrow). All images are representative of three biologically independent assays performed with similar results.
    Figure Legend Snippet: (A, F) E. coli without treatment. (B, G) Ib-M1. ( C, H, and I ) Ib-M2. (D, J) Ib-M6. (E, K) E. coli treated with PMB. The alterations are indicated as follows: cytoplasmic retraction (black bracket), bulges (white arrowhead), invagination (yellow arrow), electron-dense material (black arrow and arrowhead), lysed cells (black oval), cytoplasmic vacuoles (thin black arrow), cellular debris-lipid material (black square), and pore (white arrow). All images are representative of three biologically independent assays performed with similar results.

    Techniques Used:

    Interaction of Ib-M peptides with LPS and permeabilization of the E. coli outer membrane. (A) Determination of BODIPY-TR cadaverine displacement from LPS by Ib-M peptides after 60 min of exposure. PMB was utilized as a positive control. Values are expressed as mean ± SD of three independent assays. Statistical analysis was performed using ANOVA with Tukey’s multiple comparison test. (B) NPN fluorescence measurement upon exposure of E. coli ATCC 25922 to Ib-M1 peptide. PMB was used as the positive control at a concentration of 12.5 µM. The negative control was comprised of bacteria without the addition of peptides. Measurements were obtained at minute 60. The mean ± SD of a representative assay is presented. Significant differences were established and are denoted as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns indicates no significance.
    Figure Legend Snippet: Interaction of Ib-M peptides with LPS and permeabilization of the E. coli outer membrane. (A) Determination of BODIPY-TR cadaverine displacement from LPS by Ib-M peptides after 60 min of exposure. PMB was utilized as a positive control. Values are expressed as mean ± SD of three independent assays. Statistical analysis was performed using ANOVA with Tukey’s multiple comparison test. (B) NPN fluorescence measurement upon exposure of E. coli ATCC 25922 to Ib-M1 peptide. PMB was used as the positive control at a concentration of 12.5 µM. The negative control was comprised of bacteria without the addition of peptides. Measurements were obtained at minute 60. The mean ± SD of a representative assay is presented. Significant differences were established and are denoted as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns indicates no significance.

    Techniques Used: Membrane, Positive Control, Comparison, Fluorescence, Concentration Assay, Negative Control, Bacteria

    Inner permeabilization of E. coli ML35. ( A ) Ib-M1. ( B ) Ib-M2. ( C ) Ib-M6. Measurements were obtained every five min for 8 h. PBS without the addition of ONPG served as the negative control. ( D ) PMB and ( E ) streptomycin were employed as the positive and negative controls, respectively. Time-dependent cytoplasmic membrane depolarization of E. coli ATCC25922 induced by ( F ) Ib-M1, ( G ) Ib-M2, and ( H ) Ib-M6; as determined using the membrane potential-sensitive fluorescent dye, DiSC 3 . Dye release was monitored by measuring fluorescence at an excitation wavelength of 620 nm and an emission wavelength of 670 nm. Triton X-100 was used as the positive control. Data are expressed as mean ± SD of three independent assays.
    Figure Legend Snippet: Inner permeabilization of E. coli ML35. ( A ) Ib-M1. ( B ) Ib-M2. ( C ) Ib-M6. Measurements were obtained every five min for 8 h. PBS without the addition of ONPG served as the negative control. ( D ) PMB and ( E ) streptomycin were employed as the positive and negative controls, respectively. Time-dependent cytoplasmic membrane depolarization of E. coli ATCC25922 induced by ( F ) Ib-M1, ( G ) Ib-M2, and ( H ) Ib-M6; as determined using the membrane potential-sensitive fluorescent dye, DiSC 3 . Dye release was monitored by measuring fluorescence at an excitation wavelength of 620 nm and an emission wavelength of 670 nm. Triton X-100 was used as the positive control. Data are expressed as mean ± SD of three independent assays.

    Techniques Used: Negative Control, Membrane, Fluorescence, Positive Control

    Related Articles

    Produced:

    Article Title: Purification and characterization of a novel antibacterial peptide against Clostridium perfringens
    Article Snippet: .. The aforementioned PB6 strain produced an antibacterial peptide of 960–983 Da in size that inhibited the growth of C. perfringens ATCC 13124 and was resistant to degradation under high temperatures (100 and 121 °C) and to trypsin digestion, due to the presence of lipid or carbohydrate moieties that modified the peptide [ ]. ..

    Modification:

    Article Title: Purification and characterization of a novel antibacterial peptide against Clostridium perfringens
    Article Snippet: .. The aforementioned PB6 strain produced an antibacterial peptide of 960–983 Da in size that inhibited the growth of C. perfringens ATCC 13124 and was resistant to degradation under high temperatures (100 and 121 °C) and to trypsin digestion, due to the presence of lipid or carbohydrate moieties that modified the peptide [ ]. ..



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    Image Search Results


    (A-C) E. coli without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.

    Journal: PLOS One

    Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

    doi: 10.1371/journal.pone.0334029

    Figure Lengend Snippet: (A-C) E. coli without treatment. (D-F) Ib-M1. ( G-I ) Ib-M2. (J-L) Ib-M6. (M-O) E. coli treated with PMB. The alterations are indicated as follows: large bulges or spherical elements (asterisk), bulges in formation (white arrowhead), collapsed cells (yellow arrowhead), pores (white arrow), invaginations and deep wrinkles (yellow arrow), debris of cell membranes (white circles), and unchanged surface cells (black squares). All images are representative of three biological replicates with similar results.

    Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

    Techniques:

    (A, F) E. coli without treatment. (B, G) Ib-M1. ( C, H, and I ) Ib-M2. (D, J) Ib-M6. (E, K) E. coli treated with PMB. The alterations are indicated as follows: cytoplasmic retraction (black bracket), bulges (white arrowhead), invagination (yellow arrow), electron-dense material (black arrow and arrowhead), lysed cells (black oval), cytoplasmic vacuoles (thin black arrow), cellular debris-lipid material (black square), and pore (white arrow). All images are representative of three biologically independent assays performed with similar results.

    Journal: PLOS One

    Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

    doi: 10.1371/journal.pone.0334029

    Figure Lengend Snippet: (A, F) E. coli without treatment. (B, G) Ib-M1. ( C, H, and I ) Ib-M2. (D, J) Ib-M6. (E, K) E. coli treated with PMB. The alterations are indicated as follows: cytoplasmic retraction (black bracket), bulges (white arrowhead), invagination (yellow arrow), electron-dense material (black arrow and arrowhead), lysed cells (black oval), cytoplasmic vacuoles (thin black arrow), cellular debris-lipid material (black square), and pore (white arrow). All images are representative of three biologically independent assays performed with similar results.

    Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

    Techniques:

    Interaction of Ib-M peptides with LPS and permeabilization of the E. coli outer membrane. (A) Determination of BODIPY-TR cadaverine displacement from LPS by Ib-M peptides after 60 min of exposure. PMB was utilized as a positive control. Values are expressed as mean ± SD of three independent assays. Statistical analysis was performed using ANOVA with Tukey’s multiple comparison test. (B) NPN fluorescence measurement upon exposure of E. coli ATCC 25922 to Ib-M1 peptide. PMB was used as the positive control at a concentration of 12.5 µM. The negative control was comprised of bacteria without the addition of peptides. Measurements were obtained at minute 60. The mean ± SD of a representative assay is presented. Significant differences were established and are denoted as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns indicates no significance.

    Journal: PLOS One

    Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

    doi: 10.1371/journal.pone.0334029

    Figure Lengend Snippet: Interaction of Ib-M peptides with LPS and permeabilization of the E. coli outer membrane. (A) Determination of BODIPY-TR cadaverine displacement from LPS by Ib-M peptides after 60 min of exposure. PMB was utilized as a positive control. Values are expressed as mean ± SD of three independent assays. Statistical analysis was performed using ANOVA with Tukey’s multiple comparison test. (B) NPN fluorescence measurement upon exposure of E. coli ATCC 25922 to Ib-M1 peptide. PMB was used as the positive control at a concentration of 12.5 µM. The negative control was comprised of bacteria without the addition of peptides. Measurements were obtained at minute 60. The mean ± SD of a representative assay is presented. Significant differences were established and are denoted as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001; ns indicates no significance.

    Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

    Techniques: Membrane, Positive Control, Comparison, Fluorescence, Concentration Assay, Negative Control, Bacteria

    Inner permeabilization of E. coli ML35. ( A ) Ib-M1. ( B ) Ib-M2. ( C ) Ib-M6. Measurements were obtained every five min for 8 h. PBS without the addition of ONPG served as the negative control. ( D ) PMB and ( E ) streptomycin were employed as the positive and negative controls, respectively. Time-dependent cytoplasmic membrane depolarization of E. coli ATCC25922 induced by ( F ) Ib-M1, ( G ) Ib-M2, and ( H ) Ib-M6; as determined using the membrane potential-sensitive fluorescent dye, DiSC 3 . Dye release was monitored by measuring fluorescence at an excitation wavelength of 620 nm and an emission wavelength of 670 nm. Triton X-100 was used as the positive control. Data are expressed as mean ± SD of three independent assays.

    Journal: PLOS One

    Article Title: Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides

    doi: 10.1371/journal.pone.0334029

    Figure Lengend Snippet: Inner permeabilization of E. coli ML35. ( A ) Ib-M1. ( B ) Ib-M2. ( C ) Ib-M6. Measurements were obtained every five min for 8 h. PBS without the addition of ONPG served as the negative control. ( D ) PMB and ( E ) streptomycin were employed as the positive and negative controls, respectively. Time-dependent cytoplasmic membrane depolarization of E. coli ATCC25922 induced by ( F ) Ib-M1, ( G ) Ib-M2, and ( H ) Ib-M6; as determined using the membrane potential-sensitive fluorescent dye, DiSC 3 . Dye release was monitored by measuring fluorescence at an excitation wavelength of 620 nm and an emission wavelength of 670 nm. Triton X-100 was used as the positive control. Data are expressed as mean ± SD of three independent assays.

    Article Snippet: Collectively, our findings reveal the possible mechanisms of action of Ib-M antibacterial peptides against E. coli ATCC 25922 and provide strong scientific evidence supporting their therapeutic potential for combating bacterial pathogens.

    Techniques: Negative Control, Membrane, Fluorescence, Positive Control