Premium
MALDI‐TOF mass spectrometry of a combinatorial peptide library: effect of matrix composition on signal suppression
Author(s) -
Schlosser Gitta,
Pocsfalvi Gabriella,
Huszár Emőke,
Malorni Antonio,
Hudecz Ferenc
Publication year - 2005
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.937
Subject(s) - chemistry , mass spectrometry , electrospray ionization , matrix assisted laser desorption/ionization , matrix (chemical analysis) , peptide , pentapeptide repeat , chromatography , mass spectrum , protein mass spectrometry , cysteine , composition (language) , ionization , analytical chemistry (journal) , combinatorial chemistry , ion , organic chemistry , biochemistry , linguistics , philosophy , adsorption , desorption , enzyme
The effect of matrix composition on signal suppression caused by a dominant compound under MALDI ionization was studied using the combinatorial TQTXT pentapeptide library as a model system. The peptide library is composed of 19 components with all proteinogenic amino acids except cysteine in position X. From these compounds, only the Arg peptide (TQTRT) was detected with sufficient intensity in the MALDI‐TOF mass spectrum under typical MALDI conditions (CCA matrix). The analysis of a set of compounds utilized as different matrix components, additives and a cationizing agent revealed that the composition of the matrix is a critical point in signal suppression. Highly improved ion yields were achieved by using a CCA/DHB mixture as a matrix. The addition of K + as a cationizing agent to the CCA matrix resulted in MALDI‐TOF mass spectra with relative ion intensities very similar to those obtained by electrospray ionization. Copyright © 2005 John Wiley & Sons, Ltd.