Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone |
| |
Authors: | S Dikler JW Kelly DH Russell |
| |
Affiliation: | Department of Chemistry, Texas A & M University, College Station 77843-3255, USA. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|