Selective screening of tyrosine-nitrated peptides in tryptic mixtures by in-source photodissociation at 355 nm in matrix-assisted laser desorption ionization

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Title
Selective screening of tyrosine-nitrated peptides in tryptic mixtures by in-source photodissociation at 355 nm in matrix-assisted laser desorption ionization
Author(s)
Y S Shin; Jeong Hee Moon; M S Kim
Bibliographic Citation
Analytical Chemistry, vol. 83, no. 5, pp. 1704-1708
Publication Year
2011
Abstract
Nitration of tyrosine residues in proteins is an important post-translational modification related to various diseases such as Alzheimer's. In this work, efficient and selective photodissociation (PD) at 355 nm was observed for [M + H]+, [M + H - 16]+, and [M + H - 32]+ generated by matrix-assisted ultraviolet laser desorption ionization (UV-MALDI) of tyrosine-nitrated peptides (nitropeptides). Product ion spectra obtained by post-source PD at this wavelength contained useful information on the amino acid sequence. The spectra for nitropeptides obtained with 355 nm irradiation inside the ion source (MALDI/in-source PD) displayed characteristic triplet patterns due to PD of the above ions. For peptides displaying prominent signal in a MALDI mass map of a tryptic mixture, which are mostly those with arginine at the C-terminus, in-source PD allowed positive identification of their tyrosine-nitrated forms. Identification of such nitropeptides was possible at the 10 fmol level (in tryptic digest of 100 fmol BSA).
ISSN
0003-2700
Publisher
Amer Chem Soc
DOI
http://dx.doi.org/10.1021/ac1028352
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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