formaldehyde titration Search Results


99
ATCC mrsa 1144 s aureus 1426 esbl e coli 4493 e coli atcc 25922
Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).
Mrsa 1144 S Aureus 1426 Esbl E Coli 4493 E Coli Atcc 25922, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC e coli mg1655
Debio-1452 analogue synthesis and antibacterial activity. The general synthetic route utilized to synthesize amine-containing compounds, and their antimicrobial activities against Gram-positive and Gram-negative bacteria. (†) indicates dose-independent trailing growth observed; see Supporting Information, Extended Data Figure S1 . MIC values were determined using the microdilution broth method, as outlined by CLSI. All experiments were performed in biological triplicate. <t>E.</t> <t>coli</t> Δ tolC = JW5503.
E Coli Mg1655, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC s aureus 74cch mrsa p aeruginosa atcc 9027 candida sp
Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).
S Aureus 74cch Mrsa P Aeruginosa Atcc 9027 Candida Sp, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC fluconazole against c neoformans h99
Lipid-based systems for delivery of amphotericin B currently under development.
Fluconazole Against C Neoformans H99, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Abbott Laboratories extended release formulation of tiagabine hydrochloride
Lipid-based systems for delivery of amphotericin B currently under development.
Extended Release Formulation Of Tiagabine Hydrochloride, supplied by Abbott Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC a fumigatus
Lipid-based systems for delivery of amphotericin B currently under development.
A Fumigatus, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Metrohm AG 2 m naoh titrant
Lipid-based systems for delivery of amphotericin B currently under development.
2 M Naoh Titrant, supplied by Metrohm AG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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METTLER TOLEDO v30 volumetric kf titrator
Lipid-based systems for delivery of amphotericin B currently under development.
V30 Volumetric Kf Titrator, supplied by METTLER TOLEDO, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC c parapsilosis
Lipid-based systems for delivery of amphotericin B currently under development.
C Parapsilosis, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ATCC sln gel
Lipid-based systems for delivery of amphotericin B currently under development.
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R&D Systems biotinylated murine mbl2
(A) BLI analysis of eOD-GT8 60mer glycan variants binding to immobilized recombinant murine <t>MBL2</t> as a function of eOD particle concentration. (B–D) C57Bl/6 mice (n = 5/group) were immunized with 2 μg eOD equivalent eOD-GT8 60mer glycan variants and saponin adjuvant. Shown are average intensity Z projections through 360 μm of cleared draining lymph nodes harvested on day 7 (B, blue, CD35; red, eOD-GT8 60mer; scale bars denote 500 μm), and analyses of normalized total eOD-GT8 60mer signal per Z plane of cleared lymph nodes (C) and percent eOD-60mer signal found within follicles (D). Error bars indicate SEM; points represent average values between paired draining lymph nodes from one animal; *, p <0.05; ***, p <0.001; ****, p <0.0001, ns = not significant by one-way ANOVA followed by Tukey post hoc test.
Biotinylated Murine Mbl2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC 700221 e coli atcc 25922 p aeruginosa atcc 27853 c albicans atcc 90028
Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).
700221 E Coli Atcc 25922 P Aeruginosa Atcc 27853 C Albicans Atcc 90028, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Journal: International Journal of Molecular Sciences

Article Title: Current State of Knowledge Regarding WHO High Priority Pathogens—Resistance Mechanisms and Proposed Solutions through Candidates Such as Essential Oils: A Systematic Review

doi: 10.3390/ijms24119727

Figure Lengend Snippet: Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Article Snippet: Predoi D. et al., 2018 , MRSA 1144 S. aureus 1426 ESBL E. coli 4493 E. coli ATCC 25922 , Ocimum basilicum L. (basil) Lavandula augustifolia Mill (lavender) (linalool being the major compound in both EOs) , Broth microdilution Flow cytometric assay , Lavender EO expressed a good antibacterial action (MIC < 0.1% mg/mL for E. coli strains and up to 0.78% mg/mL for S. aureus strains; MBC < 0.1% mg/mL up to 1.56% mg/mL). The hydroxyapatite solution with lavender EO expressed an increased antibacterial activity (MIC = 0.31 mg/mL; MBC = 0.62 mg/mL for MRSA 1144), making hydroxyapatite a possible vehicle for lavender EO solutions in low concentrations. , [ ] .

Techniques: Activity Assay, Diffusion-based Assay, Inhibition, Cytotoxicity Assay, Electron Microscopy, In Vitro, Dilution Assay, Preserving, Quantitative Proteomics, Nucleic Acid Electrophoresis, Membrane, Confocal Laser Scanning Microscopy, Concentration Assay, Titration, Bacteria, Microscopy, Transmission Assay, Microdilution Assay, Produced, Modification, Clinical Proteomics, Blocking Assay, Staining, Cell Culture, Fourier Transform Infrared Spectroscopy, Spectroscopy, Reverse Transcription, Real-time Polymerase Chain Reaction, Crystal Violet Assay, Expressing, Flow Cytometry, In Vivo, Liposomes, Time-Kill Assay, Formulation, MTT Assay, Incubation, Thin Layer Chromatography, Bioassay, Antibiofilm Assay, Resazurin Assay, Biofilm Production Assay, Control, Infection, Cream, Antioxidant Activity Assay, Permeability, Virus, Extraction, Isolation

Debio-1452 analogue synthesis and antibacterial activity. The general synthetic route utilized to synthesize amine-containing compounds, and their antimicrobial activities against Gram-positive and Gram-negative bacteria. (†) indicates dose-independent trailing growth observed; see Supporting Information, Extended Data Figure S1 . MIC values were determined using the microdilution broth method, as outlined by CLSI. All experiments were performed in biological triplicate. E. coli Δ tolC = JW5503.

Journal: ACS Central Science

Article Title: An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections

doi: 10.1021/acscentsci.2c00598

Figure Lengend Snippet: Debio-1452 analogue synthesis and antibacterial activity. The general synthetic route utilized to synthesize amine-containing compounds, and their antimicrobial activities against Gram-positive and Gram-negative bacteria. (†) indicates dose-independent trailing growth observed; see Supporting Information, Extended Data Figure S1 . MIC values were determined using the microdilution broth method, as outlined by CLSI. All experiments were performed in biological triplicate. E. coli Δ tolC = JW5503.

Article Snippet: Spontaneous resistant mutants to fabimycin were generated in E. coli MG1655, A. baumannii 19606, and S. aureus ATCC 29213 at 8×, 16×, and 32× the respective MICs with low frequencies of resistance observed at 8×–16× the MIC for all pathogens ( Figure A).

Techniques: Activity Assay, Bacteria

Fabimycin mode of action studies. (A) Spontaneous resistance frequencies of S. aureus , E. coli , and A. baumannii versus fabimycin. Data represent three replicates for each pathogen with error bars representing the SEM. (B) Point mutations in FabI observed in fabimycin-resistant colonies, and the corresponding MIC values of fabimycin versus the mutants. All MICs were performed in biological triplicate.

Journal: ACS Central Science

Article Title: An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections

doi: 10.1021/acscentsci.2c00598

Figure Lengend Snippet: Fabimycin mode of action studies. (A) Spontaneous resistance frequencies of S. aureus , E. coli , and A. baumannii versus fabimycin. Data represent three replicates for each pathogen with error bars representing the SEM. (B) Point mutations in FabI observed in fabimycin-resistant colonies, and the corresponding MIC values of fabimycin versus the mutants. All MICs were performed in biological triplicate.

Article Snippet: Spontaneous resistant mutants to fabimycin were generated in E. coli MG1655, A. baumannii 19606, and S. aureus ATCC 29213 at 8×, 16×, and 32× the respective MICs with low frequencies of resistance observed at 8×–16× the MIC for all pathogens ( Figure A).

Techniques:

Computational and biophysical evaluation of fabimycin and its enantiomer. (A) Molecular dynamic simulations of fabimycin and its enantiomer using the co-crystal structures in E. coli FabI, demonstrating the enhanced flexibility (decreased stability) of ( R )-7 . (B) The determined enthalpy changes upon binding to FabI as assessed by isothermal titration calorimetry (ITC), as well as observed stabilization in a differential scanning fluorimetry assay of FabI (from E. coli and A. baumannii ) upon compound binding relative to the holoenzyme. T m values are means of technical triplicates with error shown as the standard deviation.

Journal: ACS Central Science

Article Title: An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections

doi: 10.1021/acscentsci.2c00598

Figure Lengend Snippet: Computational and biophysical evaluation of fabimycin and its enantiomer. (A) Molecular dynamic simulations of fabimycin and its enantiomer using the co-crystal structures in E. coli FabI, demonstrating the enhanced flexibility (decreased stability) of ( R )-7 . (B) The determined enthalpy changes upon binding to FabI as assessed by isothermal titration calorimetry (ITC), as well as observed stabilization in a differential scanning fluorimetry assay of FabI (from E. coli and A. baumannii ) upon compound binding relative to the holoenzyme. T m values are means of technical triplicates with error shown as the standard deviation.

Article Snippet: Spontaneous resistant mutants to fabimycin were generated in E. coli MG1655, A. baumannii 19606, and S. aureus ATCC 29213 at 8×, 16×, and 32× the respective MICs with low frequencies of resistance observed at 8×–16× the MIC for all pathogens ( Figure A).

Techniques: Binding Assay, Isothermal Titration Calorimetry, Fluorimetry Assay, Standard Deviation

Co-crystal structures of fabimycin and its enantiomer with FabI. (A) Co-crystal structure of fabimycin with E. coli FabI with NADH cofactor (PDB 7UMW ). (B) Co-crystal structure of ( R )-7 in E. coli FabI with NADH cofactor ( 7UM8 ). (C) Water network surrounding fabimycin in the E. coli FabI active site. (D) Water network surrounding ( R )-7 in the E. coli FabI active site.

Journal: ACS Central Science

Article Title: An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections

doi: 10.1021/acscentsci.2c00598

Figure Lengend Snippet: Co-crystal structures of fabimycin and its enantiomer with FabI. (A) Co-crystal structure of fabimycin with E. coli FabI with NADH cofactor (PDB 7UMW ). (B) Co-crystal structure of ( R )-7 in E. coli FabI with NADH cofactor ( 7UM8 ). (C) Water network surrounding fabimycin in the E. coli FabI active site. (D) Water network surrounding ( R )-7 in the E. coli FabI active site.

Article Snippet: Spontaneous resistant mutants to fabimycin were generated in E. coli MG1655, A. baumannii 19606, and S. aureus ATCC 29213 at 8×, 16×, and 32× the respective MICs with low frequencies of resistance observed at 8×–16× the MIC for all pathogens ( Figure A).

Techniques:

In vivo efficacy of fabimycin in a murine UTI model. After inducing diuresis, infection initiated in C3H/HeJ mice (8 per arm, 1.38 * 10 9 CFU/mouse transurethral) with E. coli AR-0055 and treated with fabimycin (IV) at varying concentrations three times daily with bacterial enumeration at 168h postinfection. Fabimycin formulated in 17% Cremophor EL, 3% SBE-β-CD in H 2 O which was the formulation used in the vehicle arm (administered intravenously on the same schedule as fabimycin). Colistin was formulated in H 2 O with 0.9% NaCl and administered subcutaneously. Percentage in red indicates the percentage of animals with bacterial counts below the limit of detection (LOD, indicated by the dotted horizontal line). In A—D statistical significance was determined by one-way ANOVA with Tukey’s multiple comparisons. NS, not significant. * P = 0.0243, *** P < 0.001, **** P < 0.0001. Data represented as the mean with s.e.m.

Journal: ACS Central Science

Article Title: An Iterative Approach Guides Discovery of the FabI Inhibitor Fabimycin, a Late-Stage Antibiotic Candidate with In Vivo Efficacy against Drug-Resistant Gram-Negative Infections

doi: 10.1021/acscentsci.2c00598

Figure Lengend Snippet: In vivo efficacy of fabimycin in a murine UTI model. After inducing diuresis, infection initiated in C3H/HeJ mice (8 per arm, 1.38 * 10 9 CFU/mouse transurethral) with E. coli AR-0055 and treated with fabimycin (IV) at varying concentrations three times daily with bacterial enumeration at 168h postinfection. Fabimycin formulated in 17% Cremophor EL, 3% SBE-β-CD in H 2 O which was the formulation used in the vehicle arm (administered intravenously on the same schedule as fabimycin). Colistin was formulated in H 2 O with 0.9% NaCl and administered subcutaneously. Percentage in red indicates the percentage of animals with bacterial counts below the limit of detection (LOD, indicated by the dotted horizontal line). In A—D statistical significance was determined by one-way ANOVA with Tukey’s multiple comparisons. NS, not significant. * P = 0.0243, *** P < 0.001, **** P < 0.0001. Data represented as the mean with s.e.m.

Article Snippet: Spontaneous resistant mutants to fabimycin were generated in E. coli MG1655, A. baumannii 19606, and S. aureus ATCC 29213 at 8×, 16×, and 32× the respective MICs with low frequencies of resistance observed at 8×–16× the MIC for all pathogens ( Figure A).

Techniques: In Vivo, Infection, Formulation

Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Journal: International Journal of Molecular Sciences

Article Title: Current State of Knowledge Regarding WHO High Priority Pathogens—Resistance Mechanisms and Proposed Solutions through Candidates Such as Essential Oils: A Systematic Review

doi: 10.3390/ijms24119727

Figure Lengend Snippet: Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Article Snippet: Marino A et al., 2020 , S. aureus ATCC 6538 S. aureus ATCC 43300 S. epidermidis ATCC 35984 L. monocytogenes ATCC 13932 B. subtilis ATCC 6633 S. aureus 7786 MRSA ( S. aureus 815) S. aureus 74CCH-MRSA P. aeruginosa ATCC 9027 Candida sp. , Coridothymus capitatus (L.) Reichenb. fil. Hydrolate alone or in association with tetracycline/itraconazole , Checkerboard method Broth microdilution Propidium iodide and MitoTracker staining , Spanish oregano (also known as Thymus capitatus (L.) Hoffmanns. and Link) EO obtained from flowers was used. Antimicrobial activity of the prepared hydrolates (alone or in combination with tetracyline and itraconazole) was assessed. The hydrolate exhibited good antimicrobial activity, as well as a synergistic action (alteration of mitochondrial function) with itraconazole against C. krusei and an additive effect (alteration of membrane permeability) with tetracycline against MRSA strains. , [ ] .

Techniques: Activity Assay, Diffusion-based Assay, Inhibition, Cytotoxicity Assay, Electron Microscopy, In Vitro, Dilution Assay, Preserving, Quantitative Proteomics, Nucleic Acid Electrophoresis, Membrane, Confocal Laser Scanning Microscopy, Concentration Assay, Titration, Bacteria, Microscopy, Transmission Assay, Microdilution Assay, Produced, Modification, Clinical Proteomics, Blocking Assay, Staining, Cell Culture, Fourier Transform Infrared Spectroscopy, Spectroscopy, Reverse Transcription, Real-time Polymerase Chain Reaction, Crystal Violet Assay, Expressing, Flow Cytometry, In Vivo, Liposomes, Time-Kill Assay, Formulation, MTT Assay, Incubation, Thin Layer Chromatography, Bioassay, Antibiofilm Assay, Resazurin Assay, Biofilm Production Assay, Control, Infection, Cream, Antioxidant Activity Assay, Permeability, Virus, Extraction, Isolation

Lipid-based systems for delivery of amphotericin B currently under development.

Journal: Pharmaceutics

Article Title: Lipid Systems for the Delivery of Amphotericin B in Antifungal Therapy

doi: 10.3390/pharmaceutics12010029

Figure Lengend Snippet: Lipid-based systems for delivery of amphotericin B currently under development.

Article Snippet: Cochleates (CAmB) , Oral , 407.3 ± 233.8 , , Soy lecithin (enriched with 50% w / w PS-CaCl 2 ): AmB (1:10 molar ratio). Aqueous-aqueous hydrogel binary system. , Oral CAmB + flucytosine more effective than oral fluconazole against C. neoformans H99 (ATCC 208821) in a murine model of cryptococcal meningoencephalitis without toxic side effects. Fluorescence imaging demonstrated brain transport and accumulation of CAmB. Oral CAmB (25 mg/kg/day) and AmB-DOC (5 mg/kg/day i.p.) plus oral flucytosine (250 mg/kg/day) for 3 weeks had similar efficacy and immunological profile in treated mice. , [ , ] .

Techniques: Formulation, Conjugation Assay, Permeability, In Vitro, Activity Assay, Produced, MTT Assay, In Vivo, Concentration Assay, Spectroscopy, Shear, Liposomes, Modification, Dispersion, Injection, Incubation, Saline, Sonication, Infection, Solubility, Encapsulation, Homogenization, Titration, Ex Vivo, Viscosity, Inhibition, Diffusion-based Assay, Emulsion, Clinical Proteomics, Fluorescence, Imaging, Adjuvant, Expressing, RNA Expression, Solvent, Control, Histopathology, Polymer, Evaporation, Emulsification, Eye Drops

Recently completed, on-going and expected clinical trials evaluating amphotericin B (AmB) safety and efficacy against antifungal and antiparasitic diseases.

Journal: Pharmaceutics

Article Title: Lipid Systems for the Delivery of Amphotericin B in Antifungal Therapy

doi: 10.3390/pharmaceutics12010029

Figure Lengend Snippet: Recently completed, on-going and expected clinical trials evaluating amphotericin B (AmB) safety and efficacy against antifungal and antiparasitic diseases.

Article Snippet: Cochleates (CAmB) , Oral , 407.3 ± 233.8 , , Soy lecithin (enriched with 50% w / w PS-CaCl 2 ): AmB (1:10 molar ratio). Aqueous-aqueous hydrogel binary system. , Oral CAmB + flucytosine more effective than oral fluconazole against C. neoformans H99 (ATCC 208821) in a murine model of cryptococcal meningoencephalitis without toxic side effects. Fluorescence imaging demonstrated brain transport and accumulation of CAmB. Oral CAmB (25 mg/kg/day) and AmB-DOC (5 mg/kg/day i.p.) plus oral flucytosine (250 mg/kg/day) for 3 weeks had similar efficacy and immunological profile in treated mice. , [ , ] .

Techniques: Clinical Proteomics, Cream, Aerosol, Saline, Capsules, Injection

Lipid-based systems for delivery of amphotericin B currently under development.

Journal: Pharmaceutics

Article Title: Lipid Systems for the Delivery of Amphotericin B in Antifungal Therapy

doi: 10.3390/pharmaceutics12010029

Figure Lengend Snippet: Lipid-based systems for delivery of amphotericin B currently under development.

Article Snippet: Nanodisk (ND) , Sinonasal (a) , 44–80 , , DMPC:DMPG (7:3 weight ratio), ApoA-I, AmB. Thin film method; sonication and dialysis after addition of AmB and ApoA-I. , HSNE exposed to toxic conc. of AmB-ND (18 h): apical membranes permeable to K + ions at 10 μg/mL AmB; reduction of apical cell K + permeability at 75 μg/mL AmB with 85% reduction of LDH and no increase in LDH release at 150 μg/mL AmB. In vitro expression of A. fumigatus (ATCC 13073) conidia after 4 h exposure to AmB-ND (10 μg/mL) smaller than exposure to AmB; AmB-ND (50 μg/mL) RNA expression without statistical significance between AmB and AmB-ND. AmB-ND protected human nasal epithelia membranes from AmB toxicity. , [ , ] .

Techniques: Formulation, Conjugation Assay, Permeability, In Vitro, Activity Assay, Produced, MTT Assay, In Vivo, Concentration Assay, Spectroscopy, Shear, Liposomes, Modification, Dispersion, Injection, Incubation, Saline, Sonication, Infection, Solubility, Encapsulation, Homogenization, Titration, Ex Vivo, Viscosity, Inhibition, Diffusion-based Assay, Emulsion, Clinical Proteomics, Fluorescence, Imaging, Adjuvant, Expressing, RNA Expression, Solvent, Control, Histopathology, Polymer, Evaporation, Emulsification, Eye Drops

Lipid-based systems for delivery of amphotericin B currently under development.

Journal: Pharmaceutics

Article Title: Lipid Systems for the Delivery of Amphotericin B in Antifungal Therapy

doi: 10.3390/pharmaceutics12010029

Figure Lengend Snippet: Lipid-based systems for delivery of amphotericin B currently under development.

Article Snippet: Castor oil-based NEs , Skin , 128.40 ± 12.71 (0.27 ± 0.05) , 95 ± 2 , 5% castor oil, 55% LAB:Plurol ® oleique (5:1), 40% Transcutol ® P, 0.50% ( w / w ) AmB; pH 7.42 ± 0.53. Aqueous titration method. , Newtonian behavior, viscosity 12.20 ± 0.28 mPa·s. In vitro sustained release (without burst effect): 100% of AmB after 75 h. AmB retention 17.76 μg/g/cm 2 after 36 h of skin application. Antifungal activity against C. albicans (ATCC 10231), C. glabrata (ATCC 66032), C. parapsilosis (ATCC 22019), A. brasiliensis (ATCC 16404), with MICs of 0.78, 0.39, 0.19, 0.13, respectively. Ex vivo permeation studies on women skin suggests no theoretical systemic absorption: all participants exhibited TEWL values in the normal range (except after 2 h, possibly caused by the effect of Transcutol ® P on skin). , [ ] .

Techniques: Formulation, Conjugation Assay, Permeability, In Vitro, Activity Assay, Produced, MTT Assay, In Vivo, Concentration Assay, Spectroscopy, Shear, Liposomes, Modification, Dispersion, Injection, Incubation, Saline, Sonication, Infection, Solubility, Encapsulation, Homogenization, Titration, Ex Vivo, Viscosity, Inhibition, Diffusion-based Assay, Emulsion, Clinical Proteomics, Fluorescence, Imaging, Adjuvant, Expressing, RNA Expression, Solvent, Control, Histopathology, Polymer, Evaporation, Emulsification, Eye Drops

Lipid-based systems for delivery of amphotericin B currently under development.

Journal: Pharmaceutics

Article Title: Lipid Systems for the Delivery of Amphotericin B in Antifungal Therapy

doi: 10.3390/pharmaceutics12010029

Figure Lengend Snippet: Lipid-based systems for delivery of amphotericin B currently under development.

Article Snippet: SLN gel , Skin , 111.1 ± 2.2 (0.13 ± 0.04) , 93.8 ± 1.8 , AmB:lipid (1:10 weight ratio), Pluronic F127 (0.25% w / v ). Solvent diffusion method in aqueous system. , Antifungal activity against Trichophyton rubrum (ATCC 28188, KWIK-STIK 0444P), ZOI (72 h) 2.81 ± 0.13 mm. Stability (ζ –23.98 ± 1.36 mV) at 2–8 °C and 25 ± 2 °C, for 3 months. AmB in aqueous phase: 90.2 ± 1.1% (compritol ATO 888), 96.5 ± 1.4% (Precirol ATO 5, selected for preparation of SLNs gel), and 72.1 ± 2.7% (stearic acid). Ex vivo permeation studies on abdomen skin of female albino Wistar rats: AmB efflux 22.34 μg/cm 2 . PII (SLN gel) 0.11 ± 0.19 Higher skin deposition, lower skin irritation, high antifungal activity, localized delivery with minimal side effects. , [ ] .

Techniques: Formulation, Conjugation Assay, Permeability, In Vitro, Activity Assay, Produced, MTT Assay, In Vivo, Concentration Assay, Spectroscopy, Shear, Liposomes, Modification, Dispersion, Injection, Incubation, Saline, Sonication, Infection, Solubility, Encapsulation, Homogenization, Titration, Ex Vivo, Viscosity, Inhibition, Diffusion-based Assay, Emulsion, Clinical Proteomics, Fluorescence, Imaging, Adjuvant, Expressing, RNA Expression, Solvent, Control, Histopathology, Polymer, Evaporation, Emulsification, Eye Drops

(A) BLI analysis of eOD-GT8 60mer glycan variants binding to immobilized recombinant murine MBL2 as a function of eOD particle concentration. (B–D) C57Bl/6 mice (n = 5/group) were immunized with 2 μg eOD equivalent eOD-GT8 60mer glycan variants and saponin adjuvant. Shown are average intensity Z projections through 360 μm of cleared draining lymph nodes harvested on day 7 (B, blue, CD35; red, eOD-GT8 60mer; scale bars denote 500 μm), and analyses of normalized total eOD-GT8 60mer signal per Z plane of cleared lymph nodes (C) and percent eOD-60mer signal found within follicles (D). Error bars indicate SEM; points represent average values between paired draining lymph nodes from one animal; *, p <0.05; ***, p <0.001; ****, p <0.0001, ns = not significant by one-way ANOVA followed by Tukey post hoc test.

Journal: Cell reports

Article Title: Mannose-binding lectin and complement mediate follicular localization and enhanced immunogenicity of diverse protein nanoparticle immunogens

doi: 10.1016/j.celrep.2021.110217

Figure Lengend Snippet: (A) BLI analysis of eOD-GT8 60mer glycan variants binding to immobilized recombinant murine MBL2 as a function of eOD particle concentration. (B–D) C57Bl/6 mice (n = 5/group) were immunized with 2 μg eOD equivalent eOD-GT8 60mer glycan variants and saponin adjuvant. Shown are average intensity Z projections through 360 μm of cleared draining lymph nodes harvested on day 7 (B, blue, CD35; red, eOD-GT8 60mer; scale bars denote 500 μm), and analyses of normalized total eOD-GT8 60mer signal per Z plane of cleared lymph nodes (C) and percent eOD-60mer signal found within follicles (D). Error bars indicate SEM; points represent average values between paired draining lymph nodes from one animal; *, p <0.05; ***, p <0.001; ****, p <0.0001, ns = not significant by one-way ANOVA followed by Tukey post hoc test.

Article Snippet: Streptavidin-coated sensors were incubated in PBS containing 1% BSA and 0.1 M CaCl and were then loaded into wells of the same solution containing 1 μg/mL biotinylated murine MBL2 (R&D Systems 2208-MB-050/CF) for 1 min.

Techniques: Glycoproteomics, Binding Assay, Recombinant, Concentration Assay, Adjuvant

(A and B) BLI binding curves of unmodified and PNGase F-treated HPV16 L1 (A) or unmodified HBsAg (B) to immobilized recombinant murine MBL2 as functions of antigen concentration. (C) C57Bl/6 mice or MBL KO mice (n = 5/group) were immunized with 0.1 μg AlexaFluor 647-labeled HPV16 L1 and saponin adjuvant. Seven days later, lymph nodes were harvested, cleared, and imaged by confocal microscopy. Shown are average intensity Z projections through 360 μm of tissue; shown is staining for CD35 (blue) and antigen (red), scale bars denote 500 μm. (D) Serum HPV16 L1-specific IgG titers over time in mice (n = 5/group) immunized with 0.1 μg HPV16 L1 and saponin adjuvant. Error bars indicate SEM, p = 0.92 compared with WT one-way ANOVA. (E) Absolute counts of germinal center B cells (B220 + GL7 + CD4 − CD38 low ) and antigen-specific germinal center B cells (B220 + GL7 + HPV16 L1 + CD4 − CD38 low ) from WT and MBL KO mice (n = 5/group) at day 12 following immunization with 0.1 μg HPV16 L1 and saponin adjuvant. Error bars indicate SEM; *, p < 0.05 by Mann-Whitney test. (F) C57BL/6 mice or MBL KO mice (n = 5/group) were immunized with 5 μg AlexaFluor 647-labeled HBsAg and saponin adjuvant. Seven days later, lymph nodes were harvested, cleared, and imaged by confocal microscopy. Shown are average intensity Z projections through 360 μm of tissue; shown is staining for CD35 (blue) and antigen (red), scale bars denote 500 μm. (G) Serum HBsAg-specific IgG titers over time in mice immunized with 5 μg HBsAg and saponin adjuvant. Error bars indicate SEM; *, p <0.05 compared with WT by one-way ANOVA followed by Tukey post hoc test. (H) Absolute counts of germinal center B cells (B220 + GL7 + CD4 − CD38 low ) and antigen-specific germinal center B cells (B220 + GL7 + HBsAg + CD4 − CD38 low ) from WT and C3 KO mice 12 days after immunization with 5 μg HBsAg and saponin adjuvant. Error bars indicate SEM; *, p <0.05 by Mann-Whitney test.

Journal: Cell reports

Article Title: Mannose-binding lectin and complement mediate follicular localization and enhanced immunogenicity of diverse protein nanoparticle immunogens

doi: 10.1016/j.celrep.2021.110217

Figure Lengend Snippet: (A and B) BLI binding curves of unmodified and PNGase F-treated HPV16 L1 (A) or unmodified HBsAg (B) to immobilized recombinant murine MBL2 as functions of antigen concentration. (C) C57Bl/6 mice or MBL KO mice (n = 5/group) were immunized with 0.1 μg AlexaFluor 647-labeled HPV16 L1 and saponin adjuvant. Seven days later, lymph nodes were harvested, cleared, and imaged by confocal microscopy. Shown are average intensity Z projections through 360 μm of tissue; shown is staining for CD35 (blue) and antigen (red), scale bars denote 500 μm. (D) Serum HPV16 L1-specific IgG titers over time in mice (n = 5/group) immunized with 0.1 μg HPV16 L1 and saponin adjuvant. Error bars indicate SEM, p = 0.92 compared with WT one-way ANOVA. (E) Absolute counts of germinal center B cells (B220 + GL7 + CD4 − CD38 low ) and antigen-specific germinal center B cells (B220 + GL7 + HPV16 L1 + CD4 − CD38 low ) from WT and MBL KO mice (n = 5/group) at day 12 following immunization with 0.1 μg HPV16 L1 and saponin adjuvant. Error bars indicate SEM; *, p < 0.05 by Mann-Whitney test. (F) C57BL/6 mice or MBL KO mice (n = 5/group) were immunized with 5 μg AlexaFluor 647-labeled HBsAg and saponin adjuvant. Seven days later, lymph nodes were harvested, cleared, and imaged by confocal microscopy. Shown are average intensity Z projections through 360 μm of tissue; shown is staining for CD35 (blue) and antigen (red), scale bars denote 500 μm. (G) Serum HBsAg-specific IgG titers over time in mice immunized with 5 μg HBsAg and saponin adjuvant. Error bars indicate SEM; *, p <0.05 compared with WT by one-way ANOVA followed by Tukey post hoc test. (H) Absolute counts of germinal center B cells (B220 + GL7 + CD4 − CD38 low ) and antigen-specific germinal center B cells (B220 + GL7 + HBsAg + CD4 − CD38 low ) from WT and C3 KO mice 12 days after immunization with 5 μg HBsAg and saponin adjuvant. Error bars indicate SEM; *, p <0.05 by Mann-Whitney test.

Article Snippet: Streptavidin-coated sensors were incubated in PBS containing 1% BSA and 0.1 M CaCl and were then loaded into wells of the same solution containing 1 μg/mL biotinylated murine MBL2 (R&D Systems 2208-MB-050/CF) for 1 min.

Techniques: Binding Assay, Recombinant, Concentration Assay, Labeling, Adjuvant, Confocal Microscopy, Staining, MANN-WHITNEY

(A) Design models of glycosylated I53–50 nanoparticles with either 240 glycans (left) or 120 glycans (right) displayed on the particle. The left particle is assembled with 20 glycosylated I53–50A trimeric subunits (protein in gray and glycans in green) and 12 non-glycosylated I53–50B pentameric subunits (orange) to display 240 glycans on the particle. The right particle is assembled with 10 glycosylated and 10 non-glycosylated I53–50A trimeric subunits, and 12 non-glycosylated I53–50B pentameric subunits to display 120 glycans. The two-component nature of I53–50 particles (i.e., each particle is composed of 20 trimers and 12 pentamers) enabled titration of glycan densities on the particle through varying the molar ratio of non-glycosylated to glycosylated I53–50A trimeric subunits; glycosylation of I53–50A trimers was either native or high-mannose for each particle formulation. (B) Mean glycan distances calculated from the particle structure for NPs with titrated levels of total glycans. (C) BLI analysis of serially glycosylated I53–50 nanoparticles binding to immobilized recombinant murine MBL2 as a function of I53–50 nanoparticle concentration. (D) The apparent dissociation constant (K D ) of immobilized murine MBL2 binding to each I53–50 high-mannose glycoform was determined by BLI analysis using a global 1:1 binding model applied to the three highest I53–50 concentrations. (E and F) C57Bl/6 mice (n = 5/group) were immunized with 5 μg I53–50 high-mannose glycan variants and saponin adjuvant. Shown are average intensity Z projections through 360 μm of cleared draining lymph nodes harvested on days 3 and 7 (E, blue, CD35; red, I53–50; scale bars denote 500 μm), and quantification of the percent I53–50 signal found within follicles (F). Error bars indicate SEM; points represent average values between paired draining lymph nodes from one animal; *, p <0.05; ****, p <0.0001, ns = not significant by one-way ANOVA followed by Tukey post hoc test. (G) Absolute counts of germinal center B cells and antigen-specific germinal center B cells from WT and MBL KO mice 12 days after immunization with 5 μg I53–50 and saponin adjuvant. Error bars indicate SEM; *, p <0.05; ns = not significant by one-way ANOVA followed by Tukey post hoc test.

Journal: Cell reports

Article Title: Mannose-binding lectin and complement mediate follicular localization and enhanced immunogenicity of diverse protein nanoparticle immunogens

doi: 10.1016/j.celrep.2021.110217

Figure Lengend Snippet: (A) Design models of glycosylated I53–50 nanoparticles with either 240 glycans (left) or 120 glycans (right) displayed on the particle. The left particle is assembled with 20 glycosylated I53–50A trimeric subunits (protein in gray and glycans in green) and 12 non-glycosylated I53–50B pentameric subunits (orange) to display 240 glycans on the particle. The right particle is assembled with 10 glycosylated and 10 non-glycosylated I53–50A trimeric subunits, and 12 non-glycosylated I53–50B pentameric subunits to display 120 glycans. The two-component nature of I53–50 particles (i.e., each particle is composed of 20 trimers and 12 pentamers) enabled titration of glycan densities on the particle through varying the molar ratio of non-glycosylated to glycosylated I53–50A trimeric subunits; glycosylation of I53–50A trimers was either native or high-mannose for each particle formulation. (B) Mean glycan distances calculated from the particle structure for NPs with titrated levels of total glycans. (C) BLI analysis of serially glycosylated I53–50 nanoparticles binding to immobilized recombinant murine MBL2 as a function of I53–50 nanoparticle concentration. (D) The apparent dissociation constant (K D ) of immobilized murine MBL2 binding to each I53–50 high-mannose glycoform was determined by BLI analysis using a global 1:1 binding model applied to the three highest I53–50 concentrations. (E and F) C57Bl/6 mice (n = 5/group) were immunized with 5 μg I53–50 high-mannose glycan variants and saponin adjuvant. Shown are average intensity Z projections through 360 μm of cleared draining lymph nodes harvested on days 3 and 7 (E, blue, CD35; red, I53–50; scale bars denote 500 μm), and quantification of the percent I53–50 signal found within follicles (F). Error bars indicate SEM; points represent average values between paired draining lymph nodes from one animal; *, p <0.05; ****, p <0.0001, ns = not significant by one-way ANOVA followed by Tukey post hoc test. (G) Absolute counts of germinal center B cells and antigen-specific germinal center B cells from WT and MBL KO mice 12 days after immunization with 5 μg I53–50 and saponin adjuvant. Error bars indicate SEM; *, p <0.05; ns = not significant by one-way ANOVA followed by Tukey post hoc test.

Article Snippet: Streptavidin-coated sensors were incubated in PBS containing 1% BSA and 0.1 M CaCl and were then loaded into wells of the same solution containing 1 μg/mL biotinylated murine MBL2 (R&D Systems 2208-MB-050/CF) for 1 min.

Techniques: Titration, Glycoproteomics, Formulation, Binding Assay, Recombinant, Concentration Assay, Adjuvant

Journal: Cell reports

Article Title: Mannose-binding lectin and complement mediate follicular localization and enhanced immunogenicity of diverse protein nanoparticle immunogens

doi: 10.1016/j.celrep.2021.110217

Figure Lengend Snippet:

Article Snippet: Streptavidin-coated sensors were incubated in PBS containing 1% BSA and 0.1 M CaCl and were then loaded into wells of the same solution containing 1 μg/mL biotinylated murine MBL2 (R&D Systems 2208-MB-050/CF) for 1 min.

Techniques: Recombinant, Staining, Antibody Labeling, Software

Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Journal: International Journal of Molecular Sciences

Article Title: Current State of Knowledge Regarding WHO High Priority Pathogens—Resistance Mechanisms and Proposed Solutions through Candidates Such as Essential Oils: A Systematic Review

doi: 10.3390/ijms24119727

Figure Lengend Snippet: Studies assessing the antimicrobial activity of essential oils against methicillin resistant, vancomycin-intermediate and -resistant S. aureus (a non-exhaustive list).

Article Snippet: Al-Maharik N et al., 2021 , MRSA S. aureus ATCC 25923 E. faecium ATCC 700221 K. pneumoniae ATCC 13883 Proteus vulgaris ATCC 700221 E. coli ATCC 25922 P. aeruginosa ATCC 27853 C. albicans ATCC 90028 , Satureja nabateorum (Danin and Hedge) Bräuchler , Broth microdilution assay Cell culture cytotoxicity assay , Both the fresh and the air-dried EOs of S. nabateorum presented good and similar antimicrobial and fungicidal activity. EO obtained from the air-dried sample manifested a higher antimicrobial activity against MRSA (MIC = 6.25 μg/mL) than ciprofloxacin (MIC = 12.5 μg/mL). Both EOs showed cytotoxic activity against HeLa and HepG2 cancer cells and were proposed as potential alternatives to bactericides and fungicides of chemical origin, as well as natural preservatives and conservation substances. , [ ] .

Techniques: Activity Assay, Diffusion-based Assay, Inhibition, Cytotoxicity Assay, Electron Microscopy, In Vitro, Dilution Assay, Preserving, Quantitative Proteomics, Nucleic Acid Electrophoresis, Membrane, Confocal Laser Scanning Microscopy, Concentration Assay, Titration, Bacteria, Microscopy, Transmission Assay, Microdilution Assay, Produced, Modification, Clinical Proteomics, Blocking Assay, Staining, Cell Culture, Fourier Transform Infrared Spectroscopy, Spectroscopy, Reverse Transcription, Real-time Polymerase Chain Reaction, Crystal Violet Assay, Expressing, Flow Cytometry, In Vivo, Liposomes, Time-Kill Assay, Formulation, MTT Assay, Incubation, Thin Layer Chromatography, Bioassay, Antibiofilm Assay, Resazurin Assay, Biofilm Production Assay, Control, Infection, Cream, Antioxidant Activity Assay, Permeability, Virus, Extraction, Isolation