Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1997 Dec;32(12):1337-49.
doi: 10.1002/(SICI)1096-9888(199712)32:12<1337::AID-JMS599>3.0.CO;2-X.

Improving Mass Spectrometric Sequencing of Arginine-Containing Peptides by Derivatization With Acetylacetone

Affiliations

Improving Mass Spectrometric Sequencing of Arginine-Containing Peptides by Derivatization With Acetylacetone

S Dikler et al. J Mass Spectrom. .

Abstract

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.

Similar articles

See all similar articles

Cited by 11 articles

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources

Feedback