Investigation of the influence of charge derivatization on the fragmentation of multiply protonated peptides.
The fragmentation of the multiply charged peptides b-chain of bovine insulin and glucagon have been investigated under low energy collision induced dissociation (CID) conditions using an electrospray ion trap mass spectrometer. The influence of charge state, specific amino acids such as aspartate or proline, the location of basic sites, and the derivatization on the fragmentation behavior has been the focus of interest. As a basis for understanding the fragmentation process, the concept of the mobile proton was applied. A set of different derivatives was used to manipulate the sites of protonation of the peptides in order to control and improve the fragmentation behavior. These results can be applied for de novo sequencing, although the sequence-specific fragmentation processes have significant influence on the dissociation behavior of the peptides.
Sonsmann
Guido
G
Institute of Biochemistry, Koln, Germany. g.sonsmann@uni.koeln.de
Römer
Axel
A
Schomburg
Dietmar
D
D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D005934:Glucagon / Q000737:chemistry; D006801:Humans; D007328:Insulin / Q000737:chemistry; D008969:Molecular Sequence Data; D009943:Organophosphorus Compounds / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D011522:Protons; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D055672:Static Electricity; D013441:Sulfinic Acids / Q000737:chemistry; D013451:Sulfonic Acids / Q000737:chemistry
D007328:Insulin; D009943:Organophosphorus Compounds; D010446:Peptide Fragments; D011522:Protons; D013441:Sulfinic Acids; D013451:Sulfonic Acids; C061896:triphenylphosphine; C013880:chlorosulfonic acid; C044255:sulfonyl chloride; D005934:Glucagon