Description:
Princeton Docket # 10-2578
Current generation fourier-transform mass spectrometers (the
Orbitrap and FTICR) coupled to online liquid chromatograpy (LC) separation and
electrospray ionization (ESI) allow quantification of thousands of ions in
complex mixtures. However, whole proteome tryptic digests, containing hundreds
of thousands of peptides, which overwhelm the capabilities of these
instruments.
Researchers in the Department of Molecular Biology, Princeton
University have developed an LTQ- Orbitrap based-method for targeted
quantification of intact peptides, specifically implementing a novel use of the
intermediate-storage only C-trap.
This invention will enable whole proteome quantification in a
single liquid chromatography mass spectrometry (LCMS) experiment by selectively
targeting specific ion populations for quantification. Specifically, this
invention will overcome current difficulties in the ability to detect low
abundant ions. A typical LC-MS/MS
experiment yields quantitative information for only around 500 of the most
highly abundant proteins from an organism.
The method described by the Princeton researchers is easily generalizable
to any ion population, and not limited to modified peptides, lipids, and
metabolites. It can potentially measure the masses and abundances for over
10,000 constituents in one complex sample. This invention will be of great
utility to biologists and other researchers, potentially enabling efficient
whole proteome quantification and could be implemented as a software enhancement
to the commercially available LTQ-Orbitrap.
Applications
Quantification of multiple ion species in complex samples
for
·
Quantitative
genetic studies
·
Drug
discovery
Advantages
·
Accurate
detection of low abundance ions
·
Increased
sensitivity
·
Enhanced
throughput
Inventor
Joshua
Bloom is
a graduate student in the Department of Molecular Biology at Princeton
University.
Intellectual Property status
Provisional application has been filed.