NDLI: $$ {{\text{C}}_{\alpha }} - {\text{C}} $$ Bond Cleavage of the Peptide Backbone in MALDI In-Source Decay Using Salicylic Acid Derivative Matrices

Content Provider	Springer Nature Link
Author	Asakawa, Daiki Takayama, Mitsuo
Copyright Year	2011
Abstract	The use of 5-formylsalicylic acid (5-FSA) and 5-nitrosalicylic acid (5-NSA) as novel matrices for in-source decay (ISD) of peptides in matrix-assisted laser desorption/ionization (MALDI) is described. The use of 5-FSA and 5-NSA generated a- and x-series ions accompanied by oxidized peptides [M – 2 H + H]$^{+}$. The preferential formation of a- and x-series ions was found to be dependent on the hydrogen-accepting ability of matrix. The hydrogen-accepting ability estimated from the ratio of signal intensity of oxidized product [M – 2 H + H]$^{+}$ to that of non-oxidized protonated molecule [M + H]$^{+}$ of peptide was of the order 5-NSA > 5-FSA > 5-aminosalicylic acid (5-ASA) ≒ 2,5-dihydroxyl benzoic acid (2,5-DHB) ≒ 0. The results suggest that the hydrogen transfer reaction from peptide to 5-FSA and 5-NSA occurs during the MALDI-ISD processes. The hydrogen abstraction from peptides results in the formation of oxidized peptides containing a radical site on the amide nitrogen with subsequent radical-induced cleavage at the $$ {{\text{C}}_{\alpha }} - {\text{C}} $$ bond, leading to the formation of a- and x-series ions. The most significant feature of MALDI-ISD with 5-FSA and 5-NSA is the specific cleavage of the $$ {{\text{C}}_{\alpha }} - {\text{C}} $$ bond of the peptide backbone without degradation of side-chain and post-translational modifications (PTM). The matrix provides a useful complementary method to conventional MALDI-ISD for amino acid sequencing and site localization of PTMs in peptides.
Starting Page	1224
Ending Page	1233
Page Count	10
File Format	PDF
ISSN	10440305
Journal	Journal of The American Society for Mass Spectrometry
Volume Number	22
Issue Number	7
e-ISSN	18791123
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-04-19
Publisher Institution	The American Society for Mass Spectrometry
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Hydrogen-accepting matrix Matrix-assisted laser desorption/ionization In-source decay Phosphorylated peptides Biotechnology Analytical Chemistry Bioinformatics Proteomics Organic Chemistry
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Structural Biology

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