INDIANAPOLIS – Building off its Orbitrap platform and a technology that allows a comparatively novel way to fragment peptides, Thermo Fisher Scientific launched two new hybrid mass spectrometers at the American Society for Mass Spectrometry conference, held here this week.
Additionally, the company announced that its high-field asymmetric waveform ion mobility spectrometry, or FAIMS, interface is now available for its ion trap mass specs. The interface allows researchers to store and fragment only those ions of interest before introducing them into the mass spectrometer, which results in less noise, increased selectivity, and better spectral quality, according to Thermo.
At a conference in which few companies made major instrument launches with proteomics applications, Thermo Fisher used ASMS as a launching pad to highlight its newest mass spec technology.
The company has used the venue for this purpose in the past. At the conference two years ago, Thermo introduced the LTQ Orbitrap, which is based on a new type of mass analyzer involving an ion trap. And at last year’s conference the company debuted its LTQ XL, the first linear ion trap mass spec with electron transfer dissociation capability.
This year, Thermo Fisher is launching the LTQ Orbitrap XL, an instrument that combines both technologies. The company also unveiled the LTQ Orbitrap Discovery mass spec here. Both instruments replace the original Orbitrap.
A comparatively new method in proteomics research, ETD provides more reliable and surer capture of phosphorylation sites. In larger peptides, it provides better sequence coverage, supporters of the method say [See PM 02.22/07].
The LTQ Orbitrap XL carries the potential to create widespread change for protein and proteomics researchers, Ian Jardine, vice president of global research and development at Thermo Fisher, told ProteoMonitor.
The instrument features the new HCD octapole collision cell for increased flexibility in MS/MS fragmentation applications, high mass accuracy and sensitivity, and up to 100,000 resolution power. It can also be upgraded to ETD capability.
As researchers start studying bigger and bigger peptides and proteins, these molecules will get to higher and higher charge states, Jardine said. The issue is that with such large ions with multiple charges, the more traditional method of collision-induced dissociation for fragmenting peptides will yield little to no information.
ETD fragments the peptides “beautifully, when you start with five, six, seven charge states, the fragments may have multiple charges,” resulting in an extremely complex fragmentation spectrum, Jardine said.
“The nominal resolution of the LTQ can’t really give you the separation of those very complex fragments,” he said.
But in an Orbitrap run at 60,000 resolution “you can interpret it beautifully. Ultimately the ability to have the kind of resolution [you can get] in the Orbitrap … as you get to bigger and bigger molecules, as you get to more charge states, that’s the way we’re going. As we go forward it’s hard for me to even imagine that we’ll think about a proteomics mass spectrometer without an embedded ETD capability.”
Thermo Fisher is currently selling the LTQ Orbitrap XL for about $600,000. The ETD option won’t be delivered for about a year, and will cost about $125,000, said Iain Mylchreest, vice president of Life Sciences Mass Spectrometry at Thermo Fisher.
A step down from the LTQ Orbitrap XL is the LTQ Orbitrap Discovery, which at less than $500,000 brings the Orbitrap technology to the price of a high-end Q-TOF, the company said. The instrument has up to 30,000 resolution power and is more suited for general proteomics work, according to company officials. While it does not have ETD capability, it can be upgraded to the LTQ Orbitrap XL, which can then be upgraded to ETD capability.
“As we go forward it’s hard for me to even imagine that we’ll think about a proteomics mass spectrometer without an embedded ETD capability.”
Thermo Fisher also launched its FAIMS technology for its ion trap mass spectrometers. According to Thermo, the interface allows researchers to store and fragment only those ions of interest before introducing them into the mass spectrometer, which results in less noise, increased selectivity, and better spectral quality.
“Most people really don’t want to look at fragmentation of single-charged ions,” Jardine said, adding that virtually all of the chemical background used in proteomic experiments is single charged. “So the simplest experiment is to tune out all of the single-charged ions so they don’t go into the mass spectrometer.
“So all you have going in there are 2+ and higher,” he said. “It means you can put a lot more ions in before you fill up, let’s say, the ion trap, so your sensitivity’s going to improve, your signal-to-noise is going to improve.”
The company also showcased this week the LCQ Fleet ion trap mass spec, launched two weeks ago, and the TSQ Quantum Ultra triple-quadrupole, launched last month. The former can be used for routine analysis of complex matrices and multicomponent systems, while the latter allows for targeted protein quantitation in complex matrices by high-throughput Highly Selective Reaction Monitoring, Thermo said.
At the conference, the company also said that it will have a new MS Masstag reagent portfolio later this year, and will introduce new protein-protein analysis protocols during the first half of 2008.
Since Thermo Electron merged with Fisher Scientific in the fall, the new firm has said little about its mass-spec business and its plans for it. Instead, in proteomics, company officials have been more vocal about its desire to expand its presence in the liquid chromatography market [See PM 01/11/07].
But Jardine said that the company continues to invest heavily in R&D in its mass specs, and the merger will benefit its mass-spec business.
“We see the merger as being incredibly positive for our mass specs, especially for our proteomics mass specs,” Jardine said.