Suppression of matrix clusters and enhancement of peptide signals in MALDI-TOF mass spectrometry using nitrilotriacetic acid.
Matrix clusters and their alkali metal ion adducts suppress peptide signals in the 500-1400 Da range and compromise MALDI-TOF mass spectrometric peptide mass fingerprinting and protein identification. Addition of 7 mM nitrilotriacetic acid to the matrix solution significantly reduced matrix clusters and increased signal-to-noise ratio of peptide signals approximately 5 to 20-fold. As a result, reliability in the identification of femtomole amounts of proteins based on peptide mass fingerprinting and database search was significantly enhanced, leading to a higher score and sequence coverage.
Kim
Jong-Seo
JS
Department of Chemistry, Seoul National University, Korea.
Kim
Ji-Young
JY
Kim
Hie-Joon
HJ
D002614:Chelating Agents; D015394:Molecular Structure; D009571:Nitrilotriacetic Acid / Q000737:chemistry*; D010455:Peptides / Q000032:analysis* / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D002614:Chelating Agents; D010455:Peptides; D009571:Nitrilotriacetic Acid