Transmission electron microscopy (TEM) and high resolution TEM (HRTEM) characterizations were performed on JEM1011 (JEOL) and JEOL-2200FS (equipped with Cs-corrector for TEM) electron microscopes with operating voltages of 100 kV and 200 kV, respectively. HAADF-STEM and EDS-mapping were performed on a JEM-ARM200F (spherical aberration correction device) electron microscope with an operating voltage of 200 kV. The XRD patterns were recorded on a PANalytical X’Pert Pro MPD diffractometer, with Cu Kα radiation (λ = 1.542 Å) at 45 kV and 40 mA. Ultraviolet–visible–near–infrared (UV–vis–NIR) absorption spectra were recorded using a U-4100 spectrophotometer (Hitachi). X-ray fluorescence (XRF) spectroscopy elemental analysis was carried out using Element Analyzer JSX-3202C (JEOL). 1H NMR spectra were measured on JEOL JNMECP300 (300 MHz) spectrometers. Matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI-TOF MS) was performed on a Bruker Autoflex Speed instrument using trans-2-[3-(4-tert-butylphenyl)-2-methyl-2-propenylidene] malononitrile (DCTB) as the matrix.
Autoflex speed instrument
Manufactured by Bruker
Sourced in Germany
The Autoflex Speed instrument is a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer designed for high-throughput analysis. It features a high-performance laser and ion detection system, enabling efficient ion generation and detection.
Automatically generated - may contain errors
Lab products found in correlation
400 mhz spectrometer, by Bruker (3 mentions)
Fla 5100, by Fujifilm (2 mentions)
Capcell pak c18 mgii, by Shiseido (2 mentions)
400 spectrometer, by Bruker (2 mentions)
Avance 3 600 spectrometer, by Bruker (2 mentions)
Microtof q 2, by Bruker (2 mentions)
X pert pro mpd diffractometer, by Malvern Panalytical (1 mentions)
Jem 1011, by JEOL (1 mentions)
U 4100 spectrophotometer, by Hitachi (1 mentions)
600 mhz nmr spectrometer, by JEOL (1 mentions)
Pu 2089plus, by Shiseido (1 mentions)
Uv 2075plus, by Shiseido (1 mentions)
Co 2067plus, by Shiseido (1 mentions)
Pu 2089plus, by Nacalai Tesque (1 mentions)
Uv 2075plus, by Nacalai Tesque (1 mentions)
Co 2065 plus, by Jasco (1 mentions)
Uv 2075 plus, by Jasco (1 mentions)
Pu 2089 plus, by Jasco (1 mentions)
Tga 4000 instrument, by PerkinElmer (1 mentions)
Flexanalysis, by Bruker (1 mentions)
11 protocols using autoflex speed instrument
1
Comprehensive Material Characterization Protocol
2
Characterization of Organic Compounds
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Materials and general procedures. All reagents and solvents were purchased from Merck (Darmstadt, Germany), J.T. Baker (Phillipsburg, NJ, USA) or Sigma-Aldrich Chemical Co. (St. Louis, MO, USA) and, unless specified, used without further purification. The melting points (m.p.) of all the compounds were determined on a SMELTING POINT 10 apparatus in open capillaries (Bibby Sterilin Ltd., Stone, UK). IR spectra were recorded on an Infralum FT-801 FTIR spectrometer (ISP SB RAS, Novosibirsk, Russia). The samples were analyzed as KBr disk solids, and the more important frequencies are shown in cm−1. 1H and 13C NMR spectra were recorded in chloroform-d3 (CDCl3) or dimethylsulfoxide-d6 (DMSO-d6) solutions at 25 °C, with a 600-MHz NMR spectrometer (JEOL Ltd., Tokyo, Japan). Peak positions were given in parts per million (ppm, δ) referenced to the appropriate solvent residual peak, and signal multiplicities were collected by: s (singlet), d (doublet), t (triplet), q (quartet), dd (doublet of doublets), br.s (broad singlet) and m (multiplet). MALDI mass spectra were recorded using a Bruker autoflex speed instrument operating in positive reflectron mode (Bremen, Germany). Elemental analyses were carried out on Euro Vector EA-3000 Elemental Analyzer (Eurovector S.p.A., Milan, Italy) for C, H and N; experimental data agreed to within 0.04% of the theoretical values.
3
Oligo Synthesis and Purification
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The general chemicals were purchased from Wako Pure Chemical, the Tokyo Chemical Institute (TCI), Aldrich, Nacalai Tesque or Kanto Kagaku. The phosphoramidites and CPGs for the DNA synthesis were purchased from the Glen Research or ChemGenes Corporation. The target oligo DNAs and RNAs were purchased from JBioS (Japan). The oligo sequences used in this study are shown in Table 1 . The HPLC purification was performed by a JASCO HPLC System (PU-2089Plus, UV-2075Plus and CO-2067Plus) using a reverse-phase C18 column (CAPCELL PAK C18 MGII, Shiseido, 4.6 × 250 mm or 10 × 250 mm). MALDI-TOF MS measurements were performed by a Bruker Autoflex speed instrument using a 3-hydroxypicolinic acid/diammonium hydrogen citrate matrix. The gel imaging and quantification were performed by a FLA-5100 (Fujifilm Co.).
4
Characterization of Oligonucleotide Compounds
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The general chemicals were purchased from Wako Pure Chemical, Aldrich or the Tokyo Chemical Institute. The target oligo DNAs and RNAs were purchased from JBioS (Japan). The oligo sequences used in this study are shown in Table 1 . The 1H NMR spectra (400 MHz) were recorded by a Bruker 400 spectrometer. The 1H NMR spectra (600 MHz) and 13C NMR spectra (150 MHz) were recorded by a Bruker AVANCE III 600 spectrometer. The high resolution electrospray mass analysis was performed by a Bruker MicrOTOFQ II. The high performance liquid chromatography (HPLC) purification was performed by a JASCO HPLC System (PU-2089Plus, UV-2075Plus, FP-2015Plus and CO-2065Plus) using a reverse-phase C18 column (COSMOSIL 5C18-AR-II, Nacalai tesque, 4.6 × 250 or 10 × 250 mm for ligand purification and CAPCELL PAK C18 MGII, Shiseido, 4.6 × 250 or 10 × 250 mm for oligo DNA purification). MALDI-TOF MS measurements were performed by a Bruker Autoflex speed instrument using a 3-hydroxypicolinic acid/diammonium hydrogen citrate matrix. The gel imaging and quantification were performed by a FLA-5100 (Fujifilm Co.).
5
Characterization of Novel Compounds
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The general chemicals were purchased from Fujifilm Wako Pure Chemical, the Tokyo Chemical Industry, Kanto Chemical or Aldrich. The target DNAs and RNAs were purchased from JBioS (Japan) (Table 1 ). The 1H NMR spectra (400 MHz) were recorded by a Bruker 400 spectrometer. The 1H NMR spectra (600 MHz) and 13C NMR spectra (150 MHz) were recorded by a Bruker AVANCE III 600 spectrometer. The high resolution electrospray mass analysis was performed by a Bruker MicrOTOFQ II. The HPLC purification was performed by a JASCO HPLC System (PU-2089Plus, UV-2075Plus, FP-2015Plus and CO-2065Plus). A reverse-phase C18 column (COSMOSIL 5C18-AR-II, Nacalai tesque, 4.6 × 250 mm or 10 × 250 mm for ligand purification). MALDI-TOF MS measurements were performed by a Bruker Autoflex speed instrument using a 3-hydroxypicolinic acid/diammonium hydrogen citrate matrix.
6
Characterization of Silver Nanoparticles
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Deuterated DDT and OT were purchased from CDN Isotopes, Inc. All other chemicals were purchased from Sigma-Aldrich and used as received. TEM images were taken using Philips CM12 operating at 100 kV. NMR spectra were recorded using Bruker 400 MHz spectrometer using CDCl3 as solvents. SAXS measurements were done using Rigaku BioSAXS 2000 machine. TGA measurements were done using TGA 4000 instrument from Perkin Elmer. Around 15 mg of nanoparticle samples were used for each measurement. The flow of nitrogen gas is at 20 ml/min and the samples were heated from 50 to 750 °C at 5.0 °C/min. The MALDI analysis on silver nanoparticle was performed using the Bruker AutoFlex Speed instrument. Chloroform solutions of around 5 mg/ml nanoparticles were prepared and mixed with an equal volume of DCTB matrix solution (20 mg/ml in chloroform). For each sample, 2 μl aliquot of such solution mixture was deposited and dried onto a stainless ground steel target plate. Measurements were performed in positive ionization mode and operated in the linear mode in the 700–3500 m/z mass range. The laser intensity was kept at around 30% for all measurements. Mass spectra were processed with FlexAnalysis (Bruker) software.
7
Characterization of Elastin-like Polypeptides by MALDI-TOF
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The molecular weight (Mw) of the ELRs was determined by MALDI-TOF-MS. Samples were dissolved in ultrapure water at 4 °C. The MALDI-TOF matrix was 2,5-dihydroxyacetophenone (2,5-DHAP). Samples were prepared by dissolving 7.6 mg of 2,5-DHAP in 375 μL of ethanol and mixing with 125 μL of an 18 mg/mL aqueous solution of C6H8O7·2NH3. 1 μL of this matrix solution was dispensed onto the MALDI plate along with 1 μL of aqueous ELR solution. The plate was dried in air and mass spectra were recorded using a Bruker autoflex speed instrument with a nitrogen laser (337 nm) operating in positive ion mode with delayed extraction.
8
Cryostat Tissue Sectioning and MALDI-MSI
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The entire R1, L and C1 segments were cut into 12-μm sections using a cryostat (Leica Microsystems, Nanterre, France). Sections obtained after every 200 μm (approx.) were subjected to MSI. These were mounted on indium tin oxide (ITO)-coated slides and placed under vacuum in a dessicator for 15 min. DHB was used as matrix, and was prepared at a concentration of 20 mg/mL in 70:30 methanol/0.1% TFA in H2O. 12 layers of matrix were deposited using SunCollect plus (SunChrom, Friedrichsdorf, Germany) programmed to spray at gradually increasing flow rates from 10 to 50 µL/min.
Lipid imaging was performed on an AutoFlex Speed instrument (Bruker Daltonics, Bremen, Germany) equipped with a FlashDetectorTM. The instrument was equipped with a Smartbeam™-II laser capable of operating up to 2 kHz and was controlled using FlexControl 3.3 (Build 108) software (Bruker Daltonics). The datasets were recorded in positive reflector mode and 500 laser shots were accumulated for each raster point. The laser focus was set to medium, and deflection of masses was deactivated. Spectra were acquired at a lateral resolution of 40 μm. External calibration was performed using the PepMix standard (Bruker Daltonics). Spectra were acquired between m/z 300–1100.
Lipid imaging was performed on an AutoFlex Speed instrument (Bruker Daltonics, Bremen, Germany) equipped with a FlashDetectorTM. The instrument was equipped with a Smartbeam™-II laser capable of operating up to 2 kHz and was controlled using FlexControl 3.3 (Build 108) software (Bruker Daltonics). The datasets were recorded in positive reflector mode and 500 laser shots were accumulated for each raster point. The laser focus was set to medium, and deflection of masses was deactivated. Spectra were acquired at a lateral resolution of 40 μm. External calibration was performed using the PepMix standard (Bruker Daltonics). Spectra were acquired between m/z 300–1100.
9
Characterization of Peptide-Porphyrin Conjugates
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The
characterization of the peptide-porphyrin conjugates involved the
acquisition of 1H NMR spectra on a Bruker (400 MHz) spectrometer,
equipped with a Bruker Sample Case autosampler. DMSOd6 served as the
solvent, and TMS was employed as the internal standard. Analytical
LC-MS was conducted on a C4, Jupiter SuC4300A, 150 × 2.00 mm2 column, utilizing a gradient of 5–100% acetonitrile
in H2O supplemented with 0.1% v/v formic acid (FA) over
a 15 min period. Matrix-assisted laser desorption/ionization time-of-flight
mass spectrometry (MALDI-TOF MS) measurements were performed using
an Autoflex Speed instrument (Bruker, Bremen, Germany), equipped with
a 355 nm Nd:YAG smartbeam laser. This laser had a maximum repetition
rate of 1000 Hz and could operate in both linear and reflector modes.
The accelerating voltage was maintained at 19 kV, with a delay time
set at 130 ns for all experiments. Mass spectra were acquired in the
reflector positive ion mode, summing spectra from 500 random laser
shots at an acquisition rate of 100 Hz. The MS spectra were calibrated
using CsI clusters with known masses.
characterization of the peptide-porphyrin conjugates involved the
acquisition of 1H NMR spectra on a Bruker (400 MHz) spectrometer,
equipped with a Bruker Sample Case autosampler. DMSOd6 served as the
solvent, and TMS was employed as the internal standard. Analytical
LC-MS was conducted on a C4, Jupiter SuC4300A, 150 × 2.00 mm2 column, utilizing a gradient of 5–100% acetonitrile
in H2O supplemented with 0.1% v/v formic acid (FA) over
a 15 min period. Matrix-assisted laser desorption/ionization time-of-flight
mass spectrometry (MALDI-TOF MS) measurements were performed using
an Autoflex Speed instrument (Bruker, Bremen, Germany), equipped with
a 355 nm Nd:YAG smartbeam laser. This laser had a maximum repetition
rate of 1000 Hz and could operate in both linear and reflector modes.
The accelerating voltage was maintained at 19 kV, with a delay time
set at 130 ns for all experiments. Mass spectra were acquired in the
reflector positive ion mode, summing spectra from 500 random laser
shots at an acquisition rate of 100 Hz. The MS spectra were calibrated
using CsI clusters with known masses.
10
Analytical Techniques for Compound Identification
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All HPLC analyses were performed on an Agilent 1260 Infinity equipped with a diode array detector and fraction collector (Agilent Technologies, Santa Clara, CA). Solvents used for the HPLC analysis were LC-MS grade and were used without further purification. Desferrioxamine standard was purchased from Sigma-Aldrich. Coproporphyrin I and III standards were purchased from Frontier Scientific. MALDI-TOF data were collected on a Bruker Autoflex Speed instrument. LC-MS/MS data were acquired using an HP1050 HPLC outfitted with a photodiode array (PDA) detector coupled to a Thermo Finnigan LCQ Advantage mass spectrometer. NMR spectra were acquired on a Bruker 400-MHz spectrometer equipped with a 5-mm PABBO z-gradient probe and referenced to residual solvent proton and carbon signals (δH 3.35, δC 49.3 for CD3OD), and LC-MS/MS analysis was performed on an Agilent 6300 ion trap. High-resolution MS1 data were collected on a Bruker Impact II quadrupole TOF (qTOF) instrument.
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