5-Amino-1-naphthol, a novel 1,5-naphthalene derivative matrix suitable for matrix-assisted laser desorption/ionization in-source decay of phosphorylated peptides
Article first published online: 21 NOV 2012
Copyright © 2012 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 27, Issue 1, pages 103–108, 15 January 2013
How to Cite
Osaka, I., Sakai, M. and Takayama, M. (2013), 5-Amino-1-naphthol, a novel 1,5-naphthalene derivative matrix suitable for matrix-assisted laser desorption/ionization in-source decay of phosphorylated peptides. Rapid Commun. Mass Spectrom., 27: 103–108. doi: 10.1002/rcm.6430
- Issue published online: 21 NOV 2012
- Article first published online: 21 NOV 2012
- Manuscript Accepted: 29 SEP 2012
- Manuscript Revised: 25 SEP 2012
- Manuscript Received: 29 JUN 2012
Although matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) is an important method for post-translational modification (PTM) analysis, the conventional matrices, 2,5-dihydroxybenzoic acid (2,5-DHB) and 1,5-diaminonaphthalene (1,5-DAN), are poor in terms of the fragment ion yields of the phosphorylated peptides. The use of 5-amino-1-naphthol (5,1-ANL) as a novel matrix for ISD of phosphorylated peptides in MALDI time-of-flight mass spectrometry (TOFMS) is described here.
We have evaluated the ion yields of ISD fragments obtained from phosphorylated peptides using three 1,5-naphthalene derivatives as MALDI-ISD matrices, i.e., 5,1-ANL, 1,5-DAN and 1,5-dihydroxynaphthalene (1,5-DHN). The signal-to-noise ratio (S/N) of c'-series ions obtained from these matrices was used to estimate their suitability for MALDI-ISD of non-modified and phosphorylated peptides.
The order of the S/N values of the ISD fragments for non-modified and phosphorylated peptides were 1,5-DAN > 5,1-ANL > 1,5-DHN and 5,1-ANL > 1,5-DHN > 1,5-DAN, respectively.
The newly introduced matrix 5,1-ANL gave highest ion yields of ISD fragments from mono-, di-, and tetraphosphorylated peptides, while 1,5-DAN was poor in the ISD ion yields for phosphorylated peptides. Copyright © 2012 John Wiley & Sons, Ltd.