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Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone

✍ Scribed by Dikler, Sergei; Kelly, Jeffery W.; Russell, David H.

Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
864 KB
Volume
32
Category
Article
ISSN
1076-5174

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✦ Synopsis

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.

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