Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry.

Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Research Abstract Details 

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Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Abstract Text:

Mikel R Roe,Hongwei Xie,Sricharan Bandhakavi,Timothy J Griffin,

The modification of proteins by the cytotoxic, reactive aldehyde 4-hydroxynonenal (HNE) is known to alter protein function and impair cellular mechanisms. In order to identify susceptible amino acid sites of HNE modification within complex biological mixtures by microcapillary liquid chromatography and linear ion trap tandem mass spectrometry, we have developed a solid-phase capture and release strategy that utilizes reversible hydrazide chemistry to enrich HNE-modified peptides. To maximize the detection of fragment ions diagnostic of HNE modification, both neutral loss-dependent acquisition of MS/MS/MS spectra and the pulsed Q dissociation operation mode were employed. When the solid-phase hydrazide enrichment strategy was applied to a yeast lysate treated with HNE, 125 distinct amino acid sites of HNE modification were mapped on 67 different proteins. The endogenous susceptibility of many of these proteins to HNE modification was demonstrated by analyzing HNE-treated yeast cell cultures with a complementary biotin hydrazide enrichment strategy. Further analysis revealed that the majority of amino acid sites susceptible to HNE modification were histidine residues, with most of these sites being flanked by basic amino acid residues, and predicted to be solvent exposed. These results demonstrate the effectiveness of this novel strategy as a general platform for proteome-scale identification of amino acid sites susceptible to HNE modification from within complex mixtures.

Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Publishing Authors By Initials

MR Roe,H Xie,S Bandhakavi,TJ Griffin,

For similar investigative techniques: chemistry, analytical: mass spectrometry: tandem mass spectrometry research abstracts see: investigative techniques: chemistry, analytical: mass spectrometry: tandem mass spectrometry research

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Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Analytical chemistry

VOLUME: 79

Page Numbers: 3747-56

Journal Abbreviation: Anal. Chem.

ISSN: 0003-2700

DAY: 17

MONTH: 04

YEAR: 2007

Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Information

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LANGUAGE: eng

NlmUniqueID: 370536

Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Keywords Mesh Terms:

KEYWORDS: Tandem Mass Spectrometry

MESH TERMS: methods

Chemical & Substance for Abstract: Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry. Information

Substance Name: 4-hydroxy-2-nonenal

Registry Number: 29343-52-0

Grant and Affiliation Information for Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase hydrazide chemistry and mass spectrometry.

AFFILIATION: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, 420 Washington Avenue SE, Minneapolis, Minnesota 55445, USA.

Country: United States

AGENCY: United States NIA

GRANT: R21-AG25371

ACRONYM: AG

MEDLINETA: Anal Chem

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