SpiralTOF™-plus Matrix-Assisted Laser Desorption/Ionization TOFMS

JMS-S3000 SpiralTOF™-plus 3.0
JMS-S3000 SpiralTOF™-plus 3.0 Matrix-Assisted Laser Desorption /Ionization Time-of-Flight Mass Spectrometer

The JMS-S3000 SpiralTOF™-plus 3.0 is a MALDI-TOFMS* that uses innovative SpiralTOF ion optics that has been updated to extend the mass range of this high resolution system. The JMS-S3000 defines a new standard in MALDI-TOFMS performance and provides state-of-the-art analytical solutions for a wide range of research areas such as functional synthetic polymers, materials science, and biomolecules.

＊Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometer

Sample Preparation for Ultra-High mass-resolution MALDI-TOFMS

Key Features

Setting the new standard in MALDI-TOFMS performance

To improve the mass resolving power and mass accuracy of a time-of-flight mass spectrometer, the flight distance must be extended while keeping a group of ions having the same m/z (an ion packet) from diverging in space. The innovative SpiralTOF™ ion optics was developed by JEOL based on  "perfect focusing" and "multi-turn" principles. The ion packets are focused back in space at every fixed distance (i.e., each figure-eight trajectory) during the flight. Thus, even after the extended flight distance, the ion packets do not diverge at the detection plane, achieving high mass resolving power, high mass accuracy, and high ion transmission.
Mass resolutions observed with a mixture of peptide standards.

Reduced topographic effect of matrix crystal

The topographic effect of the matrix crystal leads to a difference in flight start position for the ions, resulting in a difference in flight time. In the conventional ion optical system, this time difference degrades the mass resolving power and also the mass accuracy obtained with external mass calibration. With its extended flight distance, the JMS-S3000 reduces this effect to the minimum and achieves highly reproducible mass resolving power and high mass accuracy with an external mass calibration.
Another consequence of this is that high mass-resolution and mass accuracy can be maintained for imaging analysis of a biological specimen in which a large number of mass spectra are acquired across a large specimen surface that is likely to be uneven.

Achieving a wide dynamic range

The SpiralTOF™-plus 3.0 has realized a wide dynamic range by employing a 14-bit ADC (analog-to-digital converter) for TOF signal processing. This makes it possible to simultaneously detect peaks with ion intensity differences of about four orders of magnitude. Below is the measurement example of a mixture of polyethylene oxide and polypropylene oxide in the ratio of 1,000:1. In the case of polymer analysis, when combined with the Kendrick Mass Defect (KMD) analysis, it is possible to analyze trace components that are otherwise difficult to detect. In the example below, the trace component PPO was detected, and its average molecular weight and polydispersity could be calculated.
The mass spectrum of a mixture of polyethylene oxide and polypropylene oxide in the ratio of 1,000:1.

Features and usages of TOF-TOF option and linear TOF option

Features

  • By adopting the SpiralTOF™ ion optics as the first MS, the high precursor ion selectivity can be realized. The monoisotopic peak of precursor ions can be properly selected.
  • High-energy collision-induced dissociation (HE-CID) allows for the acquisition of product ion mass spectrum rich with structural information.
  • JEOL's proprietary off set parabolic reflectron technology enables the acquisition of all product ion information from m/z 5 to the precursor ion, thus facilitating the production of highly reliable structural information.

Usage

  • In structural analysis of organic compounds, the accuracy of composition determination using accurate mass in Spiral mode can be improved by determining the adduct ion, in addition to the structural information obtained by HE-CID.
  • In elucidation of amino acid sequences of a peptide, distinguishing structural isomers such as leucine and isoleucine is possible, as a feature of HE-CID. It is also possible to confirm the presence / absence of amino acids in a peptide by the presence / absence of immonium ions.
  • For the analysis of additives, surfactants, and lipids, the structural analysis of alkyl chains is important. With HE-CID, it is possible to estimate the alkyl chain length and the positions of double bonds.
  • For structural analysis of polymers, it is possible to confirm the ion type (adduct ion) and the mass of the end groups from the product ion mass spectrum. Using this information with the Spiral mode elemental composition information, the accuracy can be improved even further for structure elucidation.
Product ion mass spectrum of polypropylene oxide

Features

  • In the Linear TOF option, the ions travel from the ion source to the detector unaffected.
  • When ions undergo post source decay (PSD) in flight, the produced fragment ions and neutrals continue to fly at the same velocity as before fragmentation. Hence, in a Linear mode mass spectrum, they are detected as the same signal as that of the ions that have not fragmented. Consequently, high molecular weight compounds that tend to undergo PSD can be measured with high sensitivity using Linear mode.
  • The combination of Spiral and Linear modes further expands the range of analytes that can be measured.

Usage

  • Useful for screening of molecular weight distribution of polymers.
  • It is possible to calculate the molecular weight distribution and polydispersity of polymer samples with various masses ranging from several thousands to several hundreds of thousands.
  • It is possible to measure high-mass samples of molecular weight over 10,000 Da such as intact proteins, with high sensitivity.
  • It enables high-sensitivity measurement of samples that can easily undergo PSD, such as proteins and polysaccharides.
Mass Spectra of Bovine Serum Albumin (BSA) and Immunoglobulin G (IgG)
The linear TOF option allows easy determination of intact protein molecular weight.

Analysis Examples

Analysis of Proteins

Mass spectrum of the tryptic digest of bovine serum albumin (BSA) and the results of the peptide mass fingerprinting.

Peptide mass fingerprinting (PMF) is effective for identifying proteins isolated by two-dimensional electrophoresis. The isolated protein is digested by a protein-digesting enzyme such as trypsin, and the protein is identified by comparing the mass spectrum of the resulting peptide mixture with information in a protein database. The high mass accuracy of Spiral mode makes it possible to set an extremely narrow mass tolerance range during database matching, enabling highly reliable identification with fewer false positives.
Mass spectrum of BSA tryptic digest standard (equivalent to 500 amol)
Mass spectrum of BSA tryptic digest standard (equivalent to 500 amol)
Amount (fmol) Number of peptides matched/searched Sequence coverage (%) MASCOT score
50 52 / 81 75 570
10 41 / 79 64 390
5 36 / 77 54 351
1 28 / 57 43 255
0.5 31 / 52 46 306
0.1 12 / 34 18 92
3D-structure of RCSB PDB (www.rcsb.org) ID 1IGY (Harris, L.J., et al. (1998) J.Mol.Biol. 275: 861-872) created with Protein Workshop (Moreland, et al. (2005) BMC Bioinformatics 6:21).

Identification of Bovine Serum Albumin (BSA) by MS/MS Ion Search Method

When it is difficult to isolate a protein, identification using the MS/MS Ion Search method is effective. The entire procedure of measuring
a standard BSA tryptic digest in Spiral mode, selecting the 10 most intense ions in the measured mass spectrum as precursor ions, and
measuring each product ion mass spectrum was performed automatically. When an MS/MS Ion Search using a MASCOT Server was
performed for the 10 product ion mass spectra, BSA was identified with high confidence.

Confirmation of Synthetic Oligonucleotides

Accurate confirmation of synthetic oligonucleotides is important in the development and manufacturing of nucleic acid drugs. A synthetic oligonucleotide 5’-CGCTAAGTACGCAATGGGCC-3’ consisting of 20 bases was measured in Linear, positive ion mode and Spiral, positive ion mode. In Spiral mode, the protonated molecule [M+H]+ was observed with a mass resolution of over 40,000, with a mass measurement error of -6.4 mDa (-1.0 ppm) using the external standard method, supporting the expected elemental composition.

Structural Analysis of Oligosaccharides

High-energy collision-induced dissociation (HE-CID) tandem mass spectrometry (MS/MS) allows the identifi cation of structural isomers of oligosaccharides. Laminaritetraose and stachyose are tetrasaccharides that are structural isomers of each other. The product ion mass spectra were measured using the TOF-TOF option with sodiated molecule [M+Na]+ as the precursor ion. Although almost all product ions are common, the relative intensities of m/z 671, 658, and 599 are uniquely strong for stachyose. This is thought to refl ect the structural stress and steric hindrance unique to the 5-membered ring fructose at the reducing end of stachyose.

Structural Analysis of Phospholipids in Hen Egg Yolk

Lipids in hen egg yolk were extracted and analyzed in positive ion mode. A variety of phosphatidylcholines (PCs) were detected in the sample. In the example below, the product ion mass spectrum from the protonated molecule [M+H]+ was acquired for PC (34:1). Product ions derived from the fragmentations within the fatty acid chains were observed, which provided the information necessary for determining the fatty acid composition and double bond position.

Accurate Mass Measurements of Synthesized Organic Compounds

Previously, MALDI-TOFMS systems were not suitable for the analysis of small molecules as matrix-derived peaks and continuous chemical noise interfere with the signal from analyte molecules. The SpiralTOF ion optics have solved these problems.

Analysis of a common cold medicine

Analysis of Boroxin Cage 12-mer

Isotopic peaks are completely separated in the high-mass region due to the ultra-high mass resolving power of Spiral mode. For high molecular weight compounds, the abundance of the monoisotopic ions are very small and difficult to observe. The elemental composition of the molecule can be confirmed by the observed m/z of the most-abundant ion and/or comparing the isotopic peak pattern with that of the simulation.
Self-Assembly of Nanometer-Sized Boroxine Cages from Diboronic Acids, Ono, K., et al., J. Am. Chem. Soc. 2015, 137 (22), 7015-7018, DOI: 10.1021/jacs.5b02716

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