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Breeze 2 system

Manufactured by Waters Corporation
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The Breeze 2 system is a liquid chromatography instrument developed by Waters Corporation. It is designed to perform high-performance liquid chromatography (HPLC) analysis. The Breeze 2 system includes a solvent delivery module, an autosampler, and a UV/Vis detector. It is capable of performing various analytical tasks in a laboratory setting.

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Lab products found in correlation

400 mhz spectrometer, by Agilent Technologies (2 mentions) Qstar elite spectrometer, by Thermo Fisher Scientific (2 mentions) Cary 100 uv vis spectrophotometer, by Molecular Devices (2 mentions) Spectramax plus 384, by Molecular Devices (2 mentions) Polysorbate 80, by Merck Group (1 mentions) B16f10 cells, by American Type Culture Collection (1 mentions) Haucl4, by Merck Group (1 mentions) Nabh4, by Merck Group (1 mentions) Sodium dodecyl sulfate (sds), by Merck Group (1 mentions) Docetaxel, by LC Laboratories (1 mentions) Divinylbenzene, by Merck Group (1 mentions) Symmetry c18 column, by Waters Corporation (1 mentions) Millex gv 0.22 μm filter, by Merck Group (1 mentions) Breeze 2, by Waters Corporation (1 mentions) Minispin plus, by Eppendorf (1 mentions) Esr900 helium flow cryostat, by Oxford Instruments (1 mentions) Sx20 stopped flow spectrometer, by Applied Photophysics (1 mentions) Cary 100 bio uv vis spectrometer, by Agilent Technologies (1 mentions) E680 spectrometer, by Bruker (1 mentions) Ascend 500, by Bruker (1 mentions)

9 protocols using breeze 2 system

1

HPLC of Organic Compounds

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The HPLC was performed on a Waters Breeze 2 system equipped with a 1525 pump and 2998 PDA detector. Except for compound purification, all HPLC were performed on a Luna C18-2 column (5 μm, 4.6×250 mm) that was eluted with 40.0 mM NH4OAc (pH 4.70) and MeOH at 1.0 mL/min using a linear gradient (1) 5-30% MeOH in 0-30 min; and (2) 30-90% MeOH in 30-60 min.
Chen C., Cao R., Shrestha R., Ward C., Katz B.B., Fischer C.J., Tomich J.M, & Li P. (2015). Trapping of Intermediates with Substrate Analog HBOCoA in the Polymerizations Catalyzed by Class III Polyhydroxybutyrate (PHB) Synthase from Allochromatium Vinosum. ACS chemical biology, 10(5), 1330-1339.
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2

Synthesis and Characterization of DSPE-PCB Polymers

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DSPE-PCB 2K, 5K, and 10K were synthesized and characterized following the previously established method.35 (link) The molecular weight of NHS-PCB was characterized via Waters Breeze 2 system gel permeation chromatography (GPC) with Waters 2414 reflex detector. The mobile phase was phosphate buffered saline (PBS) at a flow rate of 1mL/min. Polysorbate 80, SDS, CTAB, HAuCl4, NaBH4, styrene, divinylbenzene, trifluoroethanol were obtained from Sigma-Aldrich. (St. Louis, USA). DSPE-PEG 5K was obtained from Laysan Bio, Inc. (Arab, USA). CB12C, CB14C, SB10C. SB16C were obtained from Anatrace Product. LLC (Maumee, USA). Docetaxel was obtained from LC Laboratories (Woburn, USA). B16F10 cells were obtained from ATCC.
Lu Y., Yue Z., Xie J., Wang W., Zhu H., Zhang E, & Cao Z. (2018). Micelles with Ultralow Critical Micelle Concentration as Carriers for Drug Delivery. Nature biomedical engineering, 2(5), 318-325.
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3

Docetaxel Micellar Formulations Development

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To prepare docetaxel/DSPE-PCB 5K formulation, 150 mg of DSPE-PCB 5K and 6 mg docetaxel were co-dissolved in 5 ml trifluoroethanol in a round-bottom flask. The solvent was subsequently evaporated by rotary evaporation to obtain a thin film. The film was then kept in a vacuum for 2 hours at room temperature to remove the residual trifluoroethanol. After the addition of 3 ml saline and stirring at 800 rpm for 30 min, a clear micelle solution with docetaxel loaded was obtained. Docetaxel/DSPE-PEG 5K and docetaxel/Polysorbate 80 formulations were prepared following the same procedure. Taxotere was prepared follow the reference63 (link), 64 (link), 69 . The weight ratios of drug over surfactant for all formulations were kept at 4%, which is the drug loading level for TAXOTERE®66 , 68 (link).
Drug release profiles were determined by placing 100 μL different formulations into Slide-A-Lyzer MINI dialysis microtubes (3500 Da MW cutoff) and dialyzed against PBS at 37°C with gentle stirring. At different time intervals, docetaxel remained in the dialyzer was quantified through HPLC by a Waters Breeze 2 System equipped with a Waters 2998 photodiode array detector at 230 nm and a Waters symmetry C18 column (4.6×7.5 mm). The mobile phase was a mixture of acetonitrile/water (50%:50% volume) at a flow rate of 1 mL/min. The docetaxel showed a single elution peak at 5.47 min.
Lu Y., Yue Z., Xie J., Wang W., Zhu H., Zhang E, & Cao Z. (2018). Micelles with Ultralow Critical Micelle Concentration as Carriers for Drug Delivery. Nature biomedical engineering, 2(5), 318-325.
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4

Analytical Characterization of Chemical Compounds

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All chemicals were purchased at the highest purity grade. All solvents were anhydrous. All reactions were performed under argon atmosphere unless otherwise specified. Thin layer chromatography (TLC) was performed using 60 mesh silica gel plates and visualization was performed using short wavelength UV light (254 nm) and basic KMnO4 staining. HPLC was performed with a Waters Breeze 2 system consisting of a 1525 pump and a 2998 photodiode array detector. Absorbance was recorded on an Agilent Cary 100 UV-Vis spectrophotometer or Molecular Devices SpectraMax Plus 384. NMR spectra were recorded on a Varian 400 MHz spectrometer. Chemical shifts of proton (1H NMR) and carbon (13C NMR) were reported in ppm relative to the residual solvent peaks except that methanol was employed as the external reference for 13C NMR when D2O was used. Chemical shifts of phosphorus (31P NMR) were reported in ppm relative to the external reference of 85% H3PO4. High resolution mass spectrometry (HRMS) was recorded on a Q-Star Elite spectrometer manufactured by Applied Biosystems.
Zhang W., Chen C., Cao R., Maurmann L, & Li P. (2014). Inhibitors to Polyhydroxyalkanoate (PHA) Synthases: Synthesis, Molecular Docking, and Implications. Chembiochem : a European journal of chemical biology, 16(1), 156-166.
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5

Peptidoglycan Muropeptide Analysis

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Macromolecular peptidoglycan was re-suspended in 500 μl of 50 mM phosphate buffer pH 4.9 and digested with Cellosyl (Hoechst AG) 100 μg/ml final concentration at 37 °C overnight. The enzyme reaction was stopped by boiling the sample for 15 min in a water bath. Coagulated protein and insoluble contamination were eliminated by centrifuging in a MiniSpin® Plus (Eppendorf) at 14,500 rpm for 15 min at room temperature. Muropeptides contained in the soluble fraction were mixed with 1/3 volume of 0.5 M sodium borate buffer (pH 9.0) and reduced with excess sodium borohydride (NaBH4) for 30 min at room temperature. The excess borohydride was neutralised with phosphoric acid (dilution 1:10) to pH 3–4. Finally the samples were filtered through Millex®-GV Filter 0.22 μm (Millipore) units and stored at −20 °C. Reduced muropeptides were separated and analysed by HPLC (Breeze™ 2 System, Waters). Elution products were detected at wavelength 204 nm and identified by the retention time obtained. The relative quantity of muropeptides present in each sample was determined by integration of their respective absorption areas (Breeze™ 2, Waters) and expressed as a molar fraction (mol%) of the total content. When required, the individual peaks were collected, vacuum dried and stored at −20 °C.
Aguilera Rossi C.G., Gómez-Puertas P, & Ayala Serrano J.A. (2016). In vivo functional and molecular characterization of the Penicillin-Binding Protein 4 (DacB) of Pseudomonas aeruginosa. BMC Microbiology, 16, 234.
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6

Isolation and Purification of Organic Compounds

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All chemicals were purchased at the highest purity grade. All solvents were anhydrous. All reactions were performed under argon atmosphere unless otherwise specified. Thin layer chromatography (TLC) was performed using 60 mesh silica gel plates and visualization was performed using short wavelength UV light (254 nm) and basic KMnO4 staining. Absorbance was recorded on an Agilent Cary 100 UV-Vis spectrophotometer or Molecular Devices SpectraMax Plus 384. NMR spectra were recorded on a Varian 400 MHz spectrometer. Chemical shifts of proton (1H NMR) and phosphorus (31P NMR) were reported in ppm relative to the residual solvent peaks and external reference of 85% H3PO4, respectively. High-resolution mass spectrometry (HRMS) was recorded on a Q-Star Elite spectrometer manufactured by Applied Biosystems.
HPLC was performed on a Waters Breeze 2 system equipped with a 1525 pump, a 2998 PDA detector, and a semi-preparative Luna C18-2 column (5 µm, 10 × 250 mm). The column was eluted at 3.0 mL/min using a linear gradient from 5% to 95% methanol in 10 mM ammonium acetate (pH 4.00) over 70 min.
Jia K., Cao R., Hua D.H, & Li P. (2016). Study of Class I and Class III Polyhydroxyalkanoate (PHA) Synthases with Substrates Containing a Modified Side Chain. Biomacromolecules, 17(4), 1477-1485.
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7

Biophysical Characterization of Oxidative Enzymes

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All activity assays and steady-state kinetics were performed on a Cary 100 Bio UV-Vis spectrometer equipped with temperature controller and magnetic stirring. Transient-state kinetics was carried out on an Applied Photophysics SX20 stopped-flow spectrometer equipped with sequential mixing, a PDA detector, and a monochromator. Analytical SEC was performed on a Waters Breeze 2 system equipped with a PDA detector. EPR spectra were recorded on a Bruker E680 spectrometer equipped with a high sensitivity cavity and an ESR900 helium flow cryostat from Oxford Instruments. All chemical and biochemical reagents were purchased at the highest grade and used without further purification. Protein concentrations were determined by BCA assays.25 (link) Stocks of H2O2 were prepared fresh before experiments and their concentrations were determined at 240 nm using ε240 = 43.6 M−1cm−1.
Shrestha R., Chen X., Ramyar K.X., Hayati Z., Carlson E.A., Bossmann S.H., Song L., Geisbrecht B.V, & Li P. (2016). Identification of Surface-Exposed Protein Radicals and A Substrate Oxidation Site in A-Class Dye-Decolorizing Peroxidase from Thermomonospora curvata. ACS catalysis, 6(12), 8036-8047.
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8

NMR Analysis of Flavonoid Compounds

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Main instruments and reagents 1 H NMR and 13 C NMR spectra of flavonoids were recorded using DMSO-d6 or methanol-d4 on a Bruker Ascend-500 spectrometer (Bruker BioSpin Gmbh, Rheinstetten, Germany) at 500 and 126 MHz, respectively. Chemical shifts were given by δ (ppm) relative to TMS as an internal reference and coupling constants (J) are reported in Hz. The preparation for HPLC and subsequent analysis were carried out using a Waters Breeze 2 system that was equipped with a 2414 refractive index detector, a 2707
Yue D., Cai W., Ding B., Zhu H., Li J., & Zhu Y. (2021). Separation and preparation of the main flavonoids in <i>Flos Dolichoris Lablab</i> and their antioxidant activity. Food Science and Technology Research, 27(3), 429-440.
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9

Ascorbic Acid Quantification in Whey using HPLC

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Ascorbic acid concentration was determined using the HPLC method outlined by Romeu-Nadal et al. (2006) . Three hundred microliters of fluid or rehydrated whey (5.0 ± 0.2% solids) was mixed with 300 μL of 0.56% (wt/vol) meta-phosphoric acid (33.5-36.5%, Sigma-Aldrich), and HPLC-grade water (Fluka) was then added. Samples were shaken for 30 s and centrifuged in a microcentrifuge at 12,000 × g for 10 min to separate fat and protein from the aqueous phase. All samples were then filtered through a 0.45-μm cellulose filter (VWR) and analyzed by HPLC (Breeze 2 system, Waters Corporation, Milford, MA) with a reversed-phase column (Kinelex 5u XB-C 18 100 × 4.60 mm, Phenomenex). Thirty microliters of sample was injected with a flow rate of 0.7 mL/min, with a mobile phase composed of HPLC-grade water with 0.1% acetic acid (Sigma-Aldrich) and methanol (HPLC grade, Fluka) at a concentration of (95:5 vol/vol). Samples were analyzed using a Waters 2998 pathodiode array detector with a wavelength of 254 nm. Ascorbic acid concentration was determined based on a 7-point standard curve derived from an l-ascorbic acid standard (≥99.0% purity, Sigma-Aldrich). All whey samples were extracted in triplicate and each extraction was injected in duplicate.
Stout M.A., Park C.W, & Drake M.A. (2017). The effect of bleaching agents on the degradation of vitamins and carotenoids in spray-dried whey protein concentrate. Journal of dairy science, 100(10).
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