Samples for Matrix assisted laser desorption ionization time-of-flight (MALDI-ToF, AXIMA Performance, Shimadzu, Manchester, UK) analysis were prepared first dissolving 5 mg of sample powder in 1 mL of a 50:50 v/v acetone/water solution. Then 10 mg of this solution is added to 10 µL of a 2,5-dihydroxy benzoic acid (DHB) matrix. The locations dedicated to the samples on the analysis plaque were first covered with 2 µL of a NaCl solution 0.1 M in 2:1 v/v methanol/water, and predried. Then 1 µL of the sample solution was placed on its dedicated location and the plaque is dried again. MALDI-ToF spectra were obtained using an Axima-Performance mass spectrometer from Shimadzu Biotech (Kratos Analytical Shimadzu Europe Ltd., Manchester, UK) using a linear polarity-positive tuning mode. The measurements were carried out making 1000 profiles per sample with two shots accumulated per profile. The spectrum precision is of +1 Da.
Axima performance
Manufactured by Shimadzu
Sourced in United Kingdom, Japan
The AXIMA Performance is a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometer designed for high-performance analysis of biomolecules. It provides accurate mass measurement and high sensitivity for a variety of applications.
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Lab products found in correlation
Sytox green, by Thermo Fisher Scientific (3 mentions)
Lsm 880, by Zeiss (2 mentions)
Lsm 900, by Zeiss (1 mentions)
Gemini 300, by Zeiss (1 mentions)
Maldi ms software, by Shimadzu (1 mentions)
20a prominence, by Shimadzu (1 mentions)
Esi it tof, by Shimadzu (1 mentions)
Labsolutions software, by Shimadzu (1 mentions)
Sil 20ac, by Shimadzu (1 mentions)
Bicinchoninic acid (bca), by Thermo Fisher Scientific (1 mentions)
Resazurin, by Merck Group (1 mentions)
Melittin, by AnaSpec (1 mentions)
Levofloxacin, by Merck Group (1 mentions)
Disc3 5, by AnaSpec (1 mentions)
Milli q synthesis a10 system, by Merck Group (1 mentions)
N methylmorpholine, by Merck Group (1 mentions)
B cereus, by American Type Culture Collection (1 mentions)
Pep 4, by GenScript (1 mentions)
α cyano 4 hydroxycinnamic acid, by Shimadzu (1 mentions)
C4 column, by Phenomenex (1 mentions)
38 protocols using axima performance
1
MALDI-ToF Analysis of Sample Powder
2
MALDI-TOF Analysis of Hydrophobic and Hydrophilic Peptides
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Example 6
In this example, 4-CHCA was used as a matrix and C8-ADHB-ES was used as an additive. For the purpose of comparison, analysis was performed using each of 4-CHCA and C8-ADHB-ES alone as a matrix.
(1) A 10 mg/mL solution (in an aqueous 50% ACN/0.05% TFA solution) of a matrix 4-CHCA and a 5 mg/mL C8-ADHB-ES solution (in an aqueous 50% ACN/0.05% TFA solution) were mixed in a ratio of 10:1 (v/v) to prepare a matrix solution (4-CHCA+C8-ADHB-ES).
(2) A 40 fmol/μL solution (in an aqueous 50% ACN/0.05% TFA solution) of a hydrophobic peptide humanin and a 40 fmol/μL solution (in an aqueous 50% ACN/0.05% TFA solution) of a hydrophilic peptide β-amyloid 1-11 were prepared and mixed in a ratio of 1:1 (v/v) to prepare a mixed solution.
(3) The sample solution (0.5 μL) prepared in (2) and the matrix solution (0.5 μL) prepared in (1) were dropped onto a MALDI plate and mixed (on-target mix).
(4) Analysis was performed using AXIMA Performance (Shimadzu Corporation) by linear TOF in positive mode.
A mass spectrum in this case is shown in
3
MALDI-TOF Analysis of Hydrophobic Peptide Humanin
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Example 5
In this example, 4-CHCA was used as a matrix and alkyl 2,5-dihydroxybenzoates (ADHB-ES) different in the length of their alkyl chain were used as additives. More specifically, C1-ADHB-ES (methyl ester), C4-ADHB-ES (butyl ester), C6-ADHB-ES (hexyl ester), C8-ADHB-ES (octyl ester), C10-ADHB-ES (decyl ester), and C16-ADHB-ES (hexadecyl ester) were used.
(1) A 10 mg/mL solution (in an aqueous 50% ACN/0.05% TFA solution) of a matrix 4-CHCA and a 5 mg/mL solution (in an aqueous 50% ACN/0.05% TFA solution) of each of C1-ADHB-ES, C4-ADHB-ES, C6-ADHB-ES, C8-ADHB-ES, C10-ADHB-ES, and C16-ADHB-ES were mixed in a ratio of 10:1 (v/v) to prepare a matrix solution. The thus obtained matrix solutions were referred to as 4-CHCA+C1-ADHB-ES, 4-CHCA+C4-ADHB-ES, 4-CHCA+C6-ADHB-ES, 4-CHCA+C8-ADHB-ES, 4-CHCA+C10-ADHB-ES, and 4-CHCA+C16-ADHB-ES, respectively.
(2) Two amol/μL to 2 pmol/μL solutions (in an aqueous 50% ACN/0.05% TFA solution) of a hydrophobic peptide humanin were prepared.
(3) Each of the sample solutions (0.5 μL) prepared in (2) and each of the matrix solutions (0.5 μL) prepared in (1) were dropped onto a MALDI plate and mixed (on-target mix).
(4) Analysis was performed using AXIMA Performance (Shimadzu Corporation) by linear TOF in positive and negative modes.
4
MALDI-TOF MS Analysis of Bacterial Proteins
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Whole bacterial proteins were analyzed using MALDI-TOF MS, as described previously (26 (link)). Cell lysates were mixed with a sinapinic acid matrix solution. MALDI mass spectra were acquired in the range of 2,000 to 30,000 m/z in positive-ion linear mode by averaging 1,000 laser shots using an AXIMA Performance (Shimadzu/Kratos, UK) equipped with a pulsed N2 laser (λ = 337 nm). Mass calibration was performed using adrenocorticotropic hormone 18 to 39 ([M + H]+, 2,466.7 m/z) and myoglobin ([M + H]+, 16,952.6 m/z; [M + 2H]2+, 8,476.8 m/z) as marker proteins of external calibration.
5
Comprehensive Microstructural Characterization
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The optical images were collected using a handheld microscope (Dino‐Lite). The microstructures were characterized using SEM (Zeiss Gemini 300) operated at 5 kV. XRD patterns were tested using Rigaku‐S2 X‐ray diffractometer. The resistance was measured by a precision source measure unit (SMU, Keysight B2912A) using the four‐probe method (Cascade EPS150FA probe station). The surface profile of the printed lines was measured using confocal laser scanning microscope (CLSM, Zeiss LSM 900). The chemical composition of tar was analyzed based on MALDI‐TOF mass spectrometry (AXIMA Performance, Shimadzu).
6
NMR and LDI-TOF-MS Characterization
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1H NMR spectra were measured on JNM-ECZ600R 600-MHz NMR spectrometer using CDCl3 as the solvent and tetramethyl silane as an internal standard at room temperature. LDI-TOF-MS measurements were conducted on Shimadzu AXIMA Performance. The applied voltage between the target and the TOF aperture is 25 kV. The sample powder was dissolved by dichloromethane without an assistant matrix. After solvent evaporation, the samples were excited by the pulsed nitrogen laser beam (337 nm) with a spot size of 0.01 mm2.
7
MALDI Analysis of GK-16 Variants
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AXIMA Performance Shimadzu was used to collect the MALDI spectra of GK-16 variants before and after enzymatic modification. α-cyano-4-hydroxycinnamic acid (CHCA) matrix of 0.7 μL was mixed with peptide solution (2 mg/mL) with a volume ratio of 1:1. All spectra were recorded under the positive mode with the linear MALDI detector.
8
MALDI-TOF Characterization of DNA Oligonucleotides
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Either
a biotinylated 31-, 83-, or 84-mer DNA sequence (100 pmol) was mixed
with 2 μL of matrix containing 1 μL of 3-hydroxy picolinic
acid (3-HPA) (50 mg/mL dissolved in acetonitrile/water 50% v/v) and
1 μL of diammonium hydrogen citrate (DAHC) (50 mg/mL dissolved
in acetonitrile/water 50% v/v). MALDI-TOF experiments were performed
using Axima Performance from Shimadzu Biotech. The mass spectrometric
measurement of 31-mer oligonucleotides was carried out in a reflectron
positive mode. The calibration of the instrument in reflectron positive
mode was performed using low-molecular-weight oligonucleotide or peptide
standard calibration kit. For high-molecular-weight oligonucleotides
(>10 000 Da), calibration was done in a linear negative
mode
using 52-, 80-, 90-, and 100-mer standards with laser power 120 in
order to enhance the signal intensity. The spectral data was processed
by using Shimadzu Biotech MALDI-MS software with processing parameters
as follows: smoothing filter width as 20 channels, baseline filter
width as 80 channels, and double threshold.
a biotinylated 31-, 83-, or 84-mer DNA sequence (100 pmol) was mixed
with 2 μL of matrix containing 1 μL of 3-hydroxy picolinic
acid (3-HPA) (50 mg/mL dissolved in acetonitrile/water 50% v/v) and
1 μL of diammonium hydrogen citrate (DAHC) (50 mg/mL dissolved
in acetonitrile/water 50% v/v). MALDI-TOF experiments were performed
using Axima Performance from Shimadzu Biotech. The mass spectrometric
measurement of 31-mer oligonucleotides was carried out in a reflectron
positive mode. The calibration of the instrument in reflectron positive
mode was performed using low-molecular-weight oligonucleotide or peptide
standard calibration kit. For high-molecular-weight oligonucleotides
(>10 000 Da), calibration was done in a linear negative
mode
using 52-, 80-, 90-, and 100-mer standards with laser power 120 in
order to enhance the signal intensity. The spectral data was processed
by using Shimadzu Biotech MALDI-MS software with processing parameters
as follows: smoothing filter width as 20 channels, baseline filter
width as 80 channels, and double threshold.
9
Mass Spectrometry Analysis of Tb II–I
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The RP-HPLC fraction was analyzed using a matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometer (Axima Performance, Shimadzu). One microliter of the sample was co-crystallized with 1 µL of α-cyano-4-hydroxycinnamic acid matrix (saturated solution prepared in 50% ACN/0.1% TFA) in the plate and dried at room temperature. The mass spectrum was obtained in the 50–15,000 mass/charge (m/z) range, in linear positive mode.
Tb II–I was also analyzed in an electrospray-ion trap-time of flight (ESI-IT-TOF) (Shimadzu Co., Kyoto, Japan) with binary ultra-fast liquid chromatography system (UFLC) (20A Prominence, Shimadzu). The sample was injected using an auto-injector module (SIL-20AC, Shimadzu), and analysis was performed in positive mode (ESI+), at a flow rate of 200 μL/min of 50% Solvent B (Solvent A: water/acetic acid (999/1, v/v); Solvent B: acetonitrile/water/acetic acid (900/99/1, v/v/v)). The interface voltage used was 4.5, and the detector voltage was 1.85 KV, with a temperature of 200 °C. Mass spectrometry ( MS) spectra were collected in the 400–1400 mass/charge rate (m/z). The data were analyzed by LabSolutions software (LCMSsolution Version 3.60.361, Shimadzu).
Tb II–I was also analyzed in an electrospray-ion trap-time of flight (ESI-IT-TOF) (Shimadzu Co., Kyoto, Japan) with binary ultra-fast liquid chromatography system (UFLC) (20A Prominence, Shimadzu). The sample was injected using an auto-injector module (SIL-20AC, Shimadzu), and analysis was performed in positive mode (ESI+), at a flow rate of 200 μL/min of 50% Solvent B (Solvent A: water/acetic acid (999/1, v/v); Solvent B: acetonitrile/water/acetic acid (900/99/1, v/v/v)). The interface voltage used was 4.5, and the detector voltage was 1.85 KV, with a temperature of 200 °C. Mass spectrometry
10
MALDI-TOF MS Analysis of Phosphorylase b
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Example 7
In this example, 4-CHCA was used as a matrix and C8-ADHB-ES was used as an additive. For the purpose of comparison, analysis was also performed using 4-CHCA alone as a matrix.
(1) A 10 mg/mL solution (in an aqueous 50% ACN/0.05% TFA solution) of a matrix 4-CHCA and a 5 mg/mL C8-ADHB-ES solution (in an aqueous 50% ACN/0.05% TFA solution) were mixed in a ratio of 10:1 (v/v) to prepare a matrix solution (4-CHCA+C8-ADHB-ES).
(2) A 200 fmol/μL solution (in an aqueous 50% ACN/0.05% TFA solution) of a tryptic digest of Phosphorylase b was prepared.
(3) The sample solution (0.5 μL) prepared in (2) and the matrix solution (0.5 μL) prepared in (1) were dropped onto a MALDI plate and mixed (on-target mix).
(4) Analysis was performed using AXIMA Performance (Shimadzu Corporation) by linear TOF in positive mode.
A mass spectrum in this case is shown in
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