efficacy against e coli atcc 25922  (ATCC)

Journal: Journal of Nanobiotechnology

Article Title: Self-assembled nanonetworks of highly stable gemini surfactant-like peptides: antibacterial mechanisms, self-assembly characteristics, and in vivo anti-infection potential

doi: 10.1186/s12951-026-04053-6

Figure Lengend Snippet: In vitro stability analysis of peptides. ( A ) Fold changes in MICs of GSLPs against E. coli 25922 and S. aureus 29213 in the presence of trypsin and pepsin (2–8 mg/mL). ( B ) MICs of IPr against E. coli 25922 and S. aureus 29213 after incubation with proteases for different times (1–4 h). ( C ) Retention of IPr after incubation with proteases for different times as determined by HPLC assay. ( D ) MICs of IPr after incubation with human serum for different times. ( E ) Physiological salt stability of IPr. Data in ( B ), ( D ) and ( E ) are presented as mean ± SEM, n = 3. No error bars indicate undetectable variation among three replicates

Article Snippet: Fortunately, IPr maintained strong bactericidal activity against both bacterial strains in the presence of seven physiological ions, with only Ca 2+ and Mg 2+ exerting a modest attenuation of its efficacy against E. coli ATCC 25922.

Techniques: In Vitro, Incubation

Journal: Journal of Nanobiotechnology

Article Title: Self-assembled nanonetworks of highly stable gemini surfactant-like peptides: antibacterial mechanisms, self-assembly characteristics, and in vivo anti-infection potential

doi: 10.1186/s12951-026-04053-6

Figure Lengend Snippet: Overall antimicrobial mechanisms of IPr. ( A ) Time-kill curves against E. coli 25922 and S. aureus 29213. ( B ) Effect of IPr on outer membrane permeability of E. coli 25922. ( C ) Effect of IPr on cytoplasmic membrane permeability of E. coli 25922. ( D ) IPr-induced cytoplasmic membrane depolarization of E. coli 25922 and S. aureus 29213. ( E ) IPr-induced inhibition of respiratory chain dehydrogenases in E. coli 25922 and S. aureus 29213. ( F ) Accumulation of intracellular ROS in E. coli 25922 and S. aureus 29213. ( G ) Extracellular ATP release in E. coli 25922 and S. aureus 29213. ( H ) Microscopic characterization of IPr-induced bacterial damage, including fluorescence microscopy with live/dead viability staining (scale bar: 400 μm and 200 μm), TEM (scale bar: 500 nm), and SEM (scale bar: 1 μm). Red arrows indicate prominent morphological damage. Data in ( A ), ( B ), ( E ), ( F ) and ( G ) are presented as mean ± SEM, n = 3. Groups with significant differences ( P < 0.05) are labeled with distinct superscripted letters (a-f). All differences between groups are analyzed by one-way ANOVA followed by Duncan post-test analysis

Article Snippet: Fortunately, IPr maintained strong bactericidal activity against both bacterial strains in the presence of seven physiological ions, with only Ca 2+ and Mg 2+ exerting a modest attenuation of its efficacy against E. coli ATCC 25922.

Techniques: Membrane, Permeability, Inhibition, Fluorescence, Microscopy, Staining, Labeling

Journal: Molecules

Article Title: Histatin 8 Interactions with Copper, Zinc, and Nickel Ions, and Its Antimicrobial Profile in Relation to Histatin 5

doi: 10.3390/molecules31010110

Figure Lengend Snippet: Growth of E. coli ATCC 25922 in the presence of Hst5 and Hst8 and copper complexes at a concentration of 200 µg/mL. C—control (peptide-free microbial culture), Hst5—histatin 5, Hst5 Cu—histatin 5 Cu complex, Hst8—histatin 8, Hst8 Cu—histatin 8 Cu complex.

Article Snippet: Hst8 had the best antibacterial efficacy against E. coli ATCC 25922, but it also inhibited the growth of S. aureus (MICs of 160μM and 320 μM, respectively).

Techniques: Concentration Assay, Control