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Principles of hydrogen radical mediated peptide/protein fragmentation during matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Asakawa Daiki
Publication year - 2014
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.21444
Subject(s) - chemistry , fourier transform ion cyclotron resonance , mass spectrometry , matrix assisted laser desorption/ionization , oxidizing agent , fragmentation (computing) , peptide , top down proteomics , proteomics , protein mass spectrometry , combinatorial chemistry , matrix (chemical analysis) , mass spectrum , analytical chemistry (journal) , desorption , chromatography , tandem mass spectrometry , biochemistry , organic chemistry , adsorption , computer science , gene , operating system
Matrix‐assisted laser desorption/ionization in‐source decay (MALDI‐ISD) is a very easy way to obtain large sequence tags and, thereby, reliable identification of peptides and proteins. Recently discovered new matrices have enhanced the MALDI‐ISD yield and opened new research avenues. The use of reducing and oxidizing matrices for MALDI‐ISD of peptides and proteins favors the production of fragmentation pathways involving “hydrogen‐abundant” and “hydrogen‐deficient” radical precursors, respectively. Since an oxidizing matrix provides information on peptide/protein sequences complementary to that obtained with a reducing matrix, MALDI‐ISD employing both reducing and oxidizing matrices is a potentially useful strategy for de novo peptide sequencing. Moreover, a pseudo‐MS 3 method provides sequence information about N‐ and C‐terminus extremities in proteins and allows N‐ and C‐terminal side fragments to be discriminated within the complex MALDI‐ISD mass spectrum. The combination of high mass resolution of a Fourier transform‐ion cyclotron resonance (FTICR) analyzer and the software suitable for MALDI‐ISD facilitates the interpretation of MALDI‐ISD mass spectra. A deeper understanding of the MALDI‐ISD process is necessary to fully exploit this method. Thus, this review focuses first on the mechanisms underlying MALDI‐ISD processes, followed by a discussion of MALDI‐ISD applications in the field of proteomics. © 2014 Wiley Periodicals, Inc., Mass Spec Rev 35:535–556, 2016