Peak capacity of ion mobility mass spectrometry: separation of peptides in helium buffer gas.
Advances in the field of proteomics depend upon the development of high-throughput separation methods. Ion mobility-mass spectrometry is a fast separation method (separations on the millisecond time-scale), which has potential for peptide complex mixture analysis. Possible disadvantages of this technique center around the lack of orthogonality between separation based on ion mobility and separation based on mass. In order to examine the utility of ion mobility-mass spectrometry, the peak capacity (phi) of the technique was estimated by subjecting a large dataset of peptides to linear regression analysis to determine an average trend for tryptic peptides. This trend-line, along with the deviation from a linear relationship observed for this dataset, was used to define the separation space for ion mobility-mass spectrometry. Using the maximum deviation found in the dataset (+/-11%) the peak capacity of ion mobility-mass spectrometry is approximately 2600 peptides. These results are discussed in light of other factors that may increase the peak capacity of ion mobility-mass spectrometry (i.e. multiple trends in the data resulting from multiple classes of compounds present in a sample) and current liquid chromatography approaches to complex peptide mixture analysis.
Ruotolo
Brandon T
BT
Laboratory for Biological Mass Spectrometry, Department of Chemistry, Texas A&M University, College Station 77843, USA.
Gillig
Kent J
KJ
Stone
Earle G
EG
Russell
David H
DH
D006371:Helium / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D010455:Peptides / Q000302:isolation & purification*; D040901:Proteomics; D014357:Trypsin / Q000737:chemistry
D010455:Peptides; D006371:Helium; D014357:Trypsin