Combination detergent/MALDI matrix: functional cleavable detergents for mass spectrometry.
This study reports the synthesis of the first functional cleavable detergent designed specifically for applications in mass spectrometry. Upon cleavage, two inert compounds and the MALDI matrix are formed, eliminating sources of potential interference originating from traditional cleavable detergents. Analysis of peptides demonstrates that MALDI matrix generated in situ results in MALDI spectra equivalent to those prepared using established protocols. Analysis of the membrane protein diacylglycerol kinase was accomplished using the combination detergent/MALDI matrix. Applications of the functional cleavable detergents to the profiling of whole cell lysates results in increased signal-to-noise ratios of many ions and the detection of additional proteins previously not observed.
Norris
Jeremy L
JL
Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37232-8575, USA.
Porter
Ned A
NA
Caprioli
Richard M
RM
D000179:Acrylates / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D002460:Cell Line; D003902:Detergents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D004926:Escherichia coli / Q000737:chemistry / Q000187:drug effects; D008565:Membrane Proteins / Q000737:chemistry; D015394:Molecular Structure; D010456:Peptides, Cyclic / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D013696:Temperature
D000179:Acrylates; D003902:Detergents; D008565:Membrane Proteins; D010456:Peptides, Cyclic; C094442:cyclic peptide 24-41C; C036658:acrylic acid