Electron transfer dissociation of amide nitrogen methylated polypeptide cations.
Unmodified and amide nitrogen methylated peptide cations were reacted with azobenzene radical anions to study the utility of electron transfer dissociation (ETD) in analyzing N-methylated peptides. We show that methylation of the amide nitrogen has no deleterious effects on the ETD process. As a result, location of alkylation on amide nitrogens should be straightforward. Such a modification might be expected to affect the ETD process if hydrogen bonding involving the amide hydrogen is important for the ETD mechanism. The partitioning of the ion/ion reaction products into all of the various reaction channels was determined and compared for modified and unmodified peptide cations. While subtle differences in the relative abundances of the various ETD channels were observed, there is no strong evidence that hydrogen bonding involving the amide nitrogen plays an important role in the ETD process.
Crizer
David M
DM
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907-2084, USA.
McLuckey
Scott A
SA
D000577:Amides / Q000737:chemistry*; D001391:Azo Compounds / Q000737:chemistry; D002412:Cations / Q000737:chemistry; D004583:Electrons; D006860:Hydrogen Bonding; D008745:Methylation; D008958:Models, Molecular; D009584:Nitrogen / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D053719:Tandem Mass Spectrometry / Q000379:methods*
D000577:Amides; D001391:Azo Compounds; D002412:Cations; D010455:Peptides; C009850:azobenzene; D009584:Nitrogen