Journal: Biology

Article Title: Antibacterial Potential of Honeybee Venom and Monascus purpureus Extracellular Metabolites Against Multidrug-Resistant Pathogenic Bacteria.

doi: 10.3390/biology14010021

Figure Lengend Snippet: Figure 1. In vitro antibacterial activity of honeybee venom (BV) extracts against three multidrug- resistant human pathogenic bacteria. (A–C) Disc diffusion method of the BV extract (200 µg·mL−1)

Article Snippet: Honeybee Venom (BV) Extract Exhibited Notable Antibacterial Activity Against MDR Human Pathogenic Bacteria Honeybee venom (BV) extract exhibited significant antibacterial activity against E. coli—ATCC 8739 (Figure 1A), S. aureus—ATCC 6538 (Figure 1B), and E. faecalis—ATCC 25923 (Figure 1C).

Techniques: In Vitro, Activity Assay, Bacteria, Diffusion-based Assay

Journal: Biology

Article Title: Antibacterial Potential of Honeybee Venom and Monascus purpureus Extracellular Metabolites Against Multidrug-Resistant Pathogenic Bacteria.

doi: 10.3390/biology14010021

Figure Lengend Snippet: Figure 2. In vitro antibacterial activity of Monascus red dye (RD) extracts against three multidrug- resistant human pathogenic bacteria. (A–C) Disc diffusion method of the RD extract (200 µg·mL−1) against Escherichia coli—ATCC 8739, Staphylococcus aureus—ATCC 6538, and Enterococcus faecalis— ATCC 25923, respectively. (D–F) Susceptibility analysis and minimum inhibitory concentrations (MICs) of RD extract against E. coli, S. aureus, and E. faecalis, respectively. Different concentrations of the RD extract were prepared in DMSO (200, 100, 50, 25, 12.5, 6.25, 3.125, 1.562, 0.781, and 0.390 µg·mL−1). (G–I) Probit regression (dose–response analysis) of RD extract against E. coli, S. au- reus, and E. faecalis, respectively. Gray dots present the means of three replicates of each concentration. Blue solid lines represent the probit regression lines, whereas red dashed lines edge represent the 95% confidence intervals for the estimated regression. Probit-associated half-maximal inhibitory concentrations (IC50; µg·L−1), 95% confidence intervals, and overall model fit are listed in Table 1. For RD extract, the IC50 against E. coli ATCC8739 was 40.876 µg·mL−1 (95% CI: 10.632–491.037 µg·mL−1), against S. aureus ATCC 6538 it was 3.131 µg·mL−1 (95% CI: 2.729–3.592 µg·mL−1), and against E. faecalis ATCC 25923 it was 18.758 µg·mL−1 (95% CI: 6.201–61.248 µg·mL−1).

Article Snippet: Honeybee Venom (BV) Extract Exhibited Notable Antibacterial Activity Against MDR Human Pathogenic Bacteria Honeybee venom (BV) extract exhibited significant antibacterial activity against E. coli—ATCC 8739 (Figure 1A), S. aureus—ATCC 6538 (Figure 1B), and E. faecalis—ATCC 25923 (Figure 1C).

Techniques: In Vitro, Activity Assay, Bacteria, Diffusion-based Assay, Concentration Assay

Journal: Biology

Article Title: Antibacterial Potential of Honeybee Venom and Monascus purpureus Extracellular Metabolites Against Multidrug-Resistant Pathogenic Bacteria.

doi: 10.3390/biology14010021

Figure Lengend Snippet: Figure 3. In vitro antibacterial activity of honeybee venom (BV) and Monascus red dye (RD) extracts against multidrug-resistant human pathogenic bacteria in comparison with traditional antibiotics. (A,B) Disc diffusion method of the BV and RD extract (200 µg·mL−1) compared with the traditional antibiotics against Escherichia coli—ATCC 8739, Staphylococcus aureus—ATCC 6538, and Enterococcus faecalis—ATCC 25923, respectively, at 24 h post-incubation (hpi) at 37 ◦C. (C–E) Inhibition zones (mm) of BV and RD extract (200 µg·mL−1) compared with traditional antibiotics against E. coli, S. au- reus, and E. faecalis, respectively. Bars and whiskers represent the means and standard deviations (Means ± SDs) of three biological replicates. Different letters signify statistically significant differences between treatments using Tukey’s HSD (p < 0.05). CIP: ciprofloxacin (5 µg), AZM: azithromycin (15 µg), S: streptomycin (10 µg), A/S: ampicillin-sulbactam (10/10 µg), and CLR: clarithromycin (15 µg).

Article Snippet: Honeybee Venom (BV) Extract Exhibited Notable Antibacterial Activity Against MDR Human Pathogenic Bacteria Honeybee venom (BV) extract exhibited significant antibacterial activity against E. coli—ATCC 8739 (Figure 1A), S. aureus—ATCC 6538 (Figure 1B), and E. faecalis—ATCC 25923 (Figure 1C).

Techniques: In Vitro, Activity Assay, Bacteria, Comparison, Diffusion-based Assay, Incubation, Inhibition

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Calcein leakage after 5 minutes from ( A ) anionic, bacteria-mimetic POPE/POPG (7:3) LUVs and ( B ) zwitterionic, erythrocyte-mimetic POPC/cholesterol (2:1) LUVs. ( C ) Depolarization of E. coli ATCC 35218 after 5-min. treatment, as monitored by diSC3-5 fluorescence. The data are representative of 3 independent experiments.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Bacteria, Fluorescence

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: In vitro activities of peptoids and peptides.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: In Vitro, Sequencing

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Scanning electron micrographs of E. coli either ( A ) without treatment, or treated for one hour with 10 μM ( B ) peptoid 1 ( C ) 1-Pro 6 , ( D ) 1 17mer , ( E ) peptoid 2, ( F ) 1 17mer alone (no bacteria), ( G ) pexiganan, or ( H ) melittin. Magnification = 50,000X.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Bacteria

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Comparison of transmission electron micrographs of transverse thin sections of representative E. coli treated for 1 hour with enough peptide or peptoid to kill some, but not all of the bacteria in the sample. ( A ) No treatment, ( B ) 10 µM pexiganan, ( C ) 100 µM melittin, ( D ) 10 µM fowlicidin-1, ( E ) 10 µM LL-37, ( F ) 10 µM peptoid 1, ( G ) 100 µM 1- N Lys 5,11 , ( H ) 100 µM 1-Pro 6 , ( I ) 10 µM 1 17mer . Images of bacteria treated with 2, 1 achiral , and 1- N sna 6,12 , are shown in Supp. Fig. . Scale bar represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Comparison, Transmission Assay, Bacteria

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Transmission electron micrographs demonstrating the co-incidence of altered and control-like morphologies in partially killed samples treated with ( A ) 10 µM LL-37 and ( B ) 10 µM peptoid 1. Soft x-ray tomography of E. coli . ( C ) Control (untreated) and ( D ) treated with 10 µM peptoid 1. Scale bar (TEM) represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Transmission Assay, Control, Tomography

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Transmission electron micrographs of E. coli treated with 100 µM peptoid 1 for ( A ) 5 minutes, ( B ) 15 minutes, ( C ) 30 minutes, and ( D ) 1 hour. 1 × 10 4 CFU/mL bacteria remained (0.01% of bacteria in the control) after 5-min treatment; all bacteria were killed after 15-min, 30-min, and 60-min treatments. Scale bar represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Transmission Assay, Bacteria, Control

Journal: Materials

Article Title: Cationic Substitutions in Hydroxyapatite: Current Status of the Derived Biofunctional Effects and Their In Vitro Interrogation Methods

doi: 10.3390/ma11112081

Figure Lengend Snippet: Synopsis of the bio-functionality realm of cation-substituted hydroxyapatites.

Article Snippet: Ce (3+) , Powder Coating , 4–20 , ○ Induces the in vitro formation of bone-like apatite in SBF; ○ In vitro cytocompatibility with L929 (for Ce-HA dose <100 μg mL −1 ) and MC3T3-E1 cell lines; ○ Cytotoxicity on pulmonary adenocarcinoma (A549) cells in Ce0.1HA, but improvement of cell viability in conjunction with strontium [ ]; ○ Antibacterial effect against S. aureus (ATCC 6538), Lactobacillus (ATCC 393), E. coli (8099), and P. aeruginosa ; enhanced zone inhibition is achieved for Gram-negative E. coli with respect to Gram-positive S. aureus . , [ , , , , , ] .

Techniques: In Vitro, Isolation, In Vivo, Animal Model, Adsorption, Concentration Assay, Modification, Dissolution, Activity Assay, Staining, Bacteria, Control, Transformation Assay

Journal: RSC Advances

Article Title: A multi-stage computational pipeline and in vitro validation for the discovery of small-molecule translation inhibitors targeting the bacterial ribosome

doi: 10.1039/d6ra01785a

Figure Lengend Snippet: Cartoon representation of E. coli 70S ribosome (PDB ID 4v7v), where small (30S) and large (50S) subunits are displayed with ribosomal proteins on the left. The investigated region, including the peptidyl transferase center on 23S rRNA, is indicated on 50S on the right. The native inhibitor Clindamycin (CLY) is shown in sticks. Mg 2+ ions in the crystal structure are depicted as magenta spheres.

Article Snippet: Among these candidates, only Mitoxantrone and Daunorubicin exhibited antibacterial activity against E. coli ATCC 10536 (Table S4–S6).

Techniques:

Journal: RSC Advances

Article Title: A multi-stage computational pipeline and in vitro validation for the discovery of small-molecule translation inhibitors targeting the bacterial ribosome

doi: 10.1039/d6ra01785a

Figure Lengend Snippet: In vitro inhibition of protein synthesis by Clindamycin (control) and the drug candidates in the E. coli cell-free translation system. Error bars represent standard error of the mean. Any error bars that are not visible are smaller than the data symbols.

Article Snippet: Among these candidates, only Mitoxantrone and Daunorubicin exhibited antibacterial activity against E. coli ATCC 10536 (Table S4–S6).

Techniques: In Vitro, Inhibition, Control

Journal: Pharmaceutics

Article Title: Periodontitis and Systemic Disorder—An Overview of Relation and Novel Treatment Modalities

doi: 10.3390/pharmaceutics13081175

Figure Lengend Snippet: A summary of periodontal formulations and their applications.

Article Snippet: Hydrogel , Polyacrylic acid (PAA) hydrogel containing metronidazole , Therapeutic dressing , Gamma-ray irradiation targeted metronidazole-loaded PAA hydrogel , The in-vitro cytocompatibility test was performed according to ISO 10993-5 and the formulation exhibited no cytotoxicity. The antibacterial activity against E. coli (ATCC 43895), S. aureus (ATCC 14458), and S. mutans (ATCC 25175) yielded satisfactory results. In release studies, metronidazole from the PAA hydrogel was consistently released and reached approximately 80% at 120 min. , [ ] .

Techniques: Activity Assay, Inhibition, Tomography, Encapsulation, Formulation, Disruption, Membrane, Produced, Infection, Derivative Assay, Expressing, Irradiation, Injection, Clarification Assay, Bacteria, Control, Polymerase Chain Reaction, In Vitro Hemolysis Assay, Transfection, MTS Assay