Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 µM, ( B ) 2 µM, ( C ) 5 µM, and ( D ) 10 µM, of peptides against logarithmic phase E. coli ATCC 25922. The graphs were generated from the representative values (average ± SE) of three independent experiments (* P < 0.05, ** P < 0.01, **** P < 0.0001 compared to untreated control).

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Analogues, Generated, Control

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Effect of higher bacterial cell densities of logarithmic phase E. coli on the killing kinetics of ( A ) KKA-MSH and ( B ) KKK-MSH against 10 6 CFU/mL, and ( C ) KKA-MSH and ( D ) KKK-MSH against 10 7 CFU/mL at different concentrations of 1 µM, 2 µM, 5 µM, and 10 µM. Each data point denotes the representative values (average ± SE) from the experiment performed on three independent days **** P < 0.0001, compared to untreated control.

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Control

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Effect of the stationary phase of E. coli cells on the killing kinetics of ( A ) α-MSH and its analogues at 10 µM concentration and ( B ) KKK-MSH at various concentrations. Experiment was repeated on three independent days, and the data was presented as mean ± SE. (**** P < 0.0001, compared to untreated control).

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Analogues, Concentration Assay, Control

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: ( A ) LPS binding affinity of α-MSH and its cationic analogues was determined by BC displacement assay. The experiment was conducted on two independent days, and each data point represents the average value ± SE. The curves were fitted as described in the Materials and Methods section. ( B ) E. coli cell mortality at a fixed concentration (10 µM) of KKK-MSH, as a function of various lipid concentrations. The experiment was conducted on three independent days, and each data point represents the average value ± SE. The experiment was performed twice, and similar data was obtained. Representative data from one set is shown here. (** P < 0.01 and **** P < 0.0001, compared to the parent peptide at corresponding concentration).

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Binding Assay, Analogues, Concentration Assay

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Peptide mediated outer membrane permeabilization of E. coli . The outer membrane permeability induced by α-MSH and its analogues was measured using the NPN (fluorescent probe) uptake assay. Data presented as average ± SE of the experiment repeated on three independent days. (** P < 0.01, *** P < 0.001, and **** P < 0.0001, compared to the parent peptide at corresponding concentration).

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Membrane, Permeability, Analogues, Concentration Assay

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Cytoplasmic membrane disruption of E. coli cells. ( A ) Instantaneous depolarization (after 2 min) by α-MSH and its analogues at different concentrations using potentiometric dye DiSC 3 (5). The experiments were performed on two different days, and mean ± SE is presented here. ( B ) Depolarization kinetics of E. coli cells on exposure to 10 µM concentration of α-MSH, KKA-MSH, KKK-MSH, and melittin. The experiment was performed twice, and similar data was obtained. Representative data from one set is shown here. ( C ) Inner membrane permeabilization of E. coli cells measured by %PI uptake in cells upon treatment with α-MSH and its analogues for 1 h. ( D ) Simultaneous E. coli cell viability check using same cell density and peptide concentrations of PI uptake experiment. The experiment was repeated on three independent days, and the average value ± SE of each data point was presented. (** P < 0.01, *** P < 0.001, and **** P < 0.0001, compared to the value for the control at the same concentration).

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Membrane, Disruption, Analogues, Concentration Assay, Control

Journal: Scientific Reports

Article Title: Binding of cationic analogues of α-MSH to lipopolysaccharide and disruption of the cytoplasmic membranes caused bactericidal action against Escherichia coli

doi: 10.1038/s41598-022-05684-z

Figure Lengend Snippet: Panel ( A ): Scanning electron micrographs and Panel ( B ): Transmission electron micrographs of E. coli ATCC 25922 after the treatment with α-MSH and its analogues at 100 µM of concentration; (a) Untreated E. coli cells, and cells treated with (b) α-MSH, (c) K-MSH, (d) KK-MSH, (e) KKA-MSH, (f) KKK-MSH, and (g) 12 µg/mL of polymyxin B at a magnification of 30,000×. Scale bar = 1 µm. Red arrows indicate the major membrane alteration sites in the peptide-treated samples.

Article Snippet: Figure 1 Killing kinetics of α-MSH and its cationic analogues at different concentrations, ( A ) 1 μM, ( B ) 2 μM, ( C ) 5 μM, and ( D ) 10 μM, of peptides against logarithmic phase E. coli ATCC 25922.

Techniques: Transmission Assay, Analogues, Concentration Assay, Membrane