Protein identification in bottom-up proteomics requires disentangling isomers of proteolytic peptides, a major class of which are sequence inversions. Separation of sequence isomers using ion mobility spectrometry (IMS) has been reported, but limited to pairs of species. Here we demonstrate baseline separation of all seven sequences for a tryptic peptide with eight residues using differential IMS or FAIMS. Evaluations of peak capacity of the method indicate that even larger libraries should generally be separated for heavier peptides with higher charge states.
Revised: September 19, 2011 |
Published: August 15, 2011
Citation
Shvartsburg A.A., A.J. Creese, R.D. Smith, and H.J. Cooper. 2011.Separation of a Set of Peptide Sequence Isomers Using Differential Ion Mobility Spectrometry.Analytical Chemistry 83, no. 18:6918-6923.PNNL-SA-81065.doi:10.1021/ac201640d