Journal:

Article Title: Geminal dialkyl derivatives of N -substituted pantothenamides: Synthesis and antibacterial activity

doi: 10.1016/j.bmc.2011.02.053

Figure Lengend Snippet: Structure of pantothenic acid and N-substituted pantothenamides

Article Snippet: A preliminary screen of these pantothenamides against other strains ( Acinetobacter baumannii ATCC 19606, Klebsiella penumoniae ATCC 13883, Escherichia coli ATCC 25922 and 11775, and Bacillus subtilis ATCC 6051 and 6633) using the agar diffusion method suggests no antimicrobial activity (inhibition zone <1.1 cm for a 1 cm disc impregnated with the desired compound). table ft1 table-wrap mode="anchored" t5 caption a7 MIC (μM) a S. aureus b MRSA c Open in a separate window 9a 7 ± 6 7± 3 Open in a separate window 9b 13 ± 7 13± 2 Open in a separate window 9c 101 ± 45 51 ± 15 Open in a separate window 9d 374 ± 187 374 ± 153 Open in a separate window 9e >715 >715 Open in a separate window 9f 3.2 ± 0.8 3.2 ± 0.9 Open in a separate window 9g >703 >703 Open in a separate window 9h >744 >744 Open in a separate window 9i 376 ± 217 376 ± 109 Open in a separate window 9j 1 ± 0.9 1 ± 0.7 Open in a separate window 9k(N5-pan) 7 ± 2 7 ± 2 Open in a separate window 9l (N9-pan) 0.4 ± 0.2 0.4 ± 0.2 Open in a separate window 9m 24 ± 14 24 ± 14 Open in a separate window a Minimum inhibitory concentrations (MICs) were determined using the following concentrations: 0.5, 1, 2, 4, 8, 16, 32, 64, 128, and 256 μg/mL.

Techniques:

Journal:

Article Title: Geminal dialkyl derivatives of N -substituted pantothenamides: Synthesis and antibacterial activity

doi: 10.1016/j.bmc.2011.02.053

Figure Lengend Snippet: Synthetic route to new N-substituted pantothenamides

Article Snippet: A preliminary screen of these pantothenamides against other strains ( Acinetobacter baumannii ATCC 19606, Klebsiella penumoniae ATCC 13883, Escherichia coli ATCC 25922 and 11775, and Bacillus subtilis ATCC 6051 and 6633) using the agar diffusion method suggests no antimicrobial activity (inhibition zone <1.1 cm for a 1 cm disc impregnated with the desired compound). table ft1 table-wrap mode="anchored" t5 caption a7 MIC (μM) a S. aureus b MRSA c Open in a separate window 9a 7 ± 6 7± 3 Open in a separate window 9b 13 ± 7 13± 2 Open in a separate window 9c 101 ± 45 51 ± 15 Open in a separate window 9d 374 ± 187 374 ± 153 Open in a separate window 9e >715 >715 Open in a separate window 9f 3.2 ± 0.8 3.2 ± 0.9 Open in a separate window 9g >703 >703 Open in a separate window 9h >744 >744 Open in a separate window 9i 376 ± 217 376 ± 109 Open in a separate window 9j 1 ± 0.9 1 ± 0.7 Open in a separate window 9k(N5-pan) 7 ± 2 7 ± 2 Open in a separate window 9l (N9-pan) 0.4 ± 0.2 0.4 ± 0.2 Open in a separate window 9m 24 ± 14 24 ± 14 Open in a separate window a Minimum inhibitory concentrations (MICs) were determined using the following concentrations: 0.5, 1, 2, 4, 8, 16, 32, 64, 128, and 256 μg/mL.

Techniques:

Journal:

Article Title: Geminal dialkyl derivatives of N -substituted pantothenamides: Synthesis and antibacterial activity

doi: 10.1016/j.bmc.2011.02.053

Figure Lengend Snippet: Antibacterial activity of N -substituted pantothenamides 9a–9m

Article Snippet: A preliminary screen of these pantothenamides against other strains ( Acinetobacter baumannii ATCC 19606, Klebsiella penumoniae ATCC 13883, Escherichia coli ATCC 25922 and 11775, and Bacillus subtilis ATCC 6051 and 6633) using the agar diffusion method suggests no antimicrobial activity (inhibition zone <1.1 cm for a 1 cm disc impregnated with the desired compound). table ft1 table-wrap mode="anchored" t5 caption a7 MIC (μM) a S. aureus b MRSA c Open in a separate window 9a 7 ± 6 7± 3 Open in a separate window 9b 13 ± 7 13± 2 Open in a separate window 9c 101 ± 45 51 ± 15 Open in a separate window 9d 374 ± 187 374 ± 153 Open in a separate window 9e >715 >715 Open in a separate window 9f 3.2 ± 0.8 3.2 ± 0.9 Open in a separate window 9g >703 >703 Open in a separate window 9h >744 >744 Open in a separate window 9i 376 ± 217 376 ± 109 Open in a separate window 9j 1 ± 0.9 1 ± 0.7 Open in a separate window 9k(N5-pan) 7 ± 2 7 ± 2 Open in a separate window 9l (N9-pan) 0.4 ± 0.2 0.4 ± 0.2 Open in a separate window 9m 24 ± 14 24 ± 14 Open in a separate window a Minimum inhibitory concentrations (MICs) were determined using the following concentrations: 0.5, 1, 2, 4, 8, 16, 32, 64, 128, and 256 μg/mL.

Techniques: Activity Assay

Journal: Antimicrobial Agents and Chemotherapy

Article Title: First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae

doi: 10.1128/AAC.00282-18

Figure Lengend Snippet: Relative expression of different PBPs in K. pneumoniae strains ATCC 43816 and ATCC 13883. Labeled PBPs were separated on SDS-PAGE gels and quantified using the ImageQuantTL software. Data are the average ± SD of results from triplicates for the PBP expression relative to that of PBP5/6.

Article Snippet: We studied, in duplicate, two K. pneumoniae strains (ATCC 43816 and ATCC 13883) which have minimal β-lactamase activity.

Techniques: Expressing, Labeling, SDS Page, Software

Journal: Antimicrobial Agents and Chemotherapy

Article Title: First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae

doi: 10.1128/AAC.00282-18

Figure Lengend Snippet: Binding patterns of β-lactams (see Table 1, footnote a, for abbreviations) for K. pneumoniae PBPs from strain ATCC 43816. The indicated β-lactam concentrations were used during the 30-min binding reaction before Bocillin FL was added. Labeled PBPs were separated by SDS-PAGE and detected using a fluorimager. A large range of β-lactam concentrations was captured using two different gels (left, 0.007 to 1 mg/liter; right, 2 to 128 mg/liter) for each drug.

Article Snippet: We studied, in duplicate, two K. pneumoniae strains (ATCC 43816 and ATCC 13883) which have minimal β-lactamase activity.

Techniques: Binding Assay, Labeling, SDS Page

Journal: Antimicrobial Agents and Chemotherapy

Article Title: First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae

doi: 10.1128/AAC.00282-18

Figure Lengend Snippet: Binding patterns of β-lactams for K. pneumoniae PBPs from strain ATCC 13883 (as described in the legend to Fig. 3).

Article Snippet: We studied, in duplicate, two K. pneumoniae strains (ATCC 43816 and ATCC 13883) which have minimal β-lactamase activity.

Techniques: Binding Assay

Journal: Antimicrobial Agents and Chemotherapy

Article Title: First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae

doi: 10.1128/AAC.00282-18

Figure Lengend Snippet: Binding patterns of β-lactamase inhibitors for K. pneumoniae PBPs from strains ATCC 43816 and ATCC 13883 (as described in the legend to Fig. 3).

Article Snippet: We studied, in duplicate, two K. pneumoniae strains (ATCC 43816 and ATCC 13883) which have minimal β-lactamase activity.

Techniques: Binding Assay

Journal: Antimicrobial Agents and Chemotherapy

Article Title: First Penicillin-Binding Protein Occupancy Patterns of β-Lactams and β-Lactamase Inhibitors in Klebsiella pneumoniae

doi: 10.1128/AAC.00282-18

Figure Lengend Snippet: Principal component analysis of the log-transformed PBP IC50 data for our 13 tested compounds in two K. pneumoniae strains. The plot shows the clustering of compounds according to their positions on the first and second eigenvector. These two vectors explained 86.5% of the total variance. Compounds were grouped into two general clusters. The first cluster contained β-lactams that primarily targeted PBP3 but differed in their secondary targets. The second cluster was comprised of compounds that primarily targeted PBP2 or both PBPs 2 and 4. Of note, among compounds in the second cluster, the carbapenems, amoxicillin, and mecillinam had substantially lower IC50 for their primary targets than the β-lactamase inhibitors. Symbols for β-lactamase inhibitors are smaller due to their much higher IC50 for their primary PBP target relative to the primary PBP target IC50 of the β-lactams.

Article Snippet: We studied, in duplicate, two K. pneumoniae strains (ATCC 43816 and ATCC 13883) which have minimal β-lactamase activity.

Techniques: Transformation Assay