Protease-dependent fractional mass and peptide properties.
Mass spectrometric analyses of peptides mainly rely on cleavage of proteins with proteases that have a defined specificity. The specificities of the proteases imply that there is not a random distribution of amino acids in the peptides. The physico-chemical effects of this distribution have been partly analyzed for tryptic peptides, but to a lesser degree for other proteases. Using all human proteins in Swiss-Prot, the relationships between peptide fractional mass, pI and hydrophobicity were investigated. The distribution of the fractional masses and the average regression lines for the fractional masses were similar, but not identical, for the peptides generated by the proteases trypsin, chymotrypsin and gluC, with the steepest regression line for gluC. The fractional mass regression lines for individual proteins showed up to +/-100 ppm in mass difference from the average regression line and the peptides generated showed protease-dependent properties. We here show that the fractional mass and some other properties of the peptides are dependent on the protease used for generating the peptides. With the increasing accuracy of mass spectrometry instruments it is possible to exploit the information embedded in the fractional mass of unknown peaks in peptide mass fingerprint spectra.
Barsnes
Harald
H
Department of Informatics, University of Bergen, Norway. Harald.Barsnes@ii.uib.no
Eidhammer
Ingvar
I
Cruciani
Véronique
V
Mikalsen
Svein-Ole
SO
D002918:Chymotrypsin / Q000378:metabolism; D030562:Databases, Protein; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007526:Isoelectric Point; D013058:Mass Spectrometry; D008970:Molecular Weight; D010449:Peptide Mapping / Q000379:methods*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D012044:Regression Analysis; D014357:Trypsin / Q000378:metabolism
D010455:Peptides; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin