Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone.
Modification of arginine residues in bradykinin, [1-5]-bradykinin, splenopentin and two synthetic pentapeptides with acetylacetone (pentane-2,4-dione) significantly increases the relative abundance of sequence-specific fragment ions produced by matrix-assisted laser desorption/ionization (MALDI). The fragmentation efficiency as measured by post-source decay in a reflectron time-of-flight mass spectrometer increases by a factor of 2-3.5. Peptide bonds adjacent to modified residues are more susceptible to cleavage than in the non-derivatized peptide ions. The increased lability of these bonds gives rise to more complete sequence information. In addition, the relative abundances of sequence-specific fragment ions are enhanced. This strategy makes it possible to obtain valuable structural information from arginine-containing peptides that otherwise do not fragment well.
Dikler
S
S
Department of Chemistry, Texas A & M University, College Station 77843-3255, USA.
Kelly
J W
JW
Russell
D H
DH
D001120:Arginine / Q000032:analysis*; D001920:Bradykinin / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D013058:Mass Spectrometry; D010422:Pentanones / Q000737:chemistry*; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides / Q000032:analysis*; D017421:Sequence Analysis; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013056:Spectrophotometry, Ultraviolet; D013946:Thymopoietins / Q000032:analysis
D010422:Pentanones; D010446:Peptide Fragments; D010455:Peptides; D013946:Thymopoietins; C008790:acetylacetone; C041898:splenopentin; D001120:Arginine; D001920:Bradykinin