N-terminal H3/D3-acetylation for improved high-throughput peptide sequencing by matrix-assisted laser desorption/ionization mass spectrometry with a time-of-flight/time-of-flight analyzer

A novel method for peptide sequencing by matrix‐assisted laser desorption/ionization mass spectrometry with a time‐of‐flight/time‐of‐flight analyzer (MALDI‐TOF/TOF) is presented. A stable isotope label introduced in the peptide N‐terminus by derivatization, using a 1:1 mixture of acetic anhydride an...

Full description

Saved in:
Bibliographic Details
Published in:Rapid communications in mass spectrometry 2006, Vol.20 (12), p.1823-1827
Main Authors: Noga, Marek J., Asperger, Arndt, Silberring, Jerzy
Format: Article
Language:English
Subjects:
Acetylation
Deuterium - chemistry
Microchemistry - methods
Peptide Mapping - methods
Proteomics - instrumentation
Proteomics - methods
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - instrumentation
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Tandem Mass Spectrometry - methods
Tritium - chemistry
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A novel method for peptide sequencing by matrix‐assisted laser desorption/ionization mass spectrometry with a time‐of‐flight/time‐of‐flight analyzer (MALDI‐TOF/TOF) is presented. A stable isotope label introduced in the peptide N‐terminus by derivatization, using a 1:1 mixture of acetic anhydride and deuterated acetic anhydride, allows for easy and unambiguous identification of ions belonging either to the N‐ or the C‐terminal ion series in the product ion spectrum, making sequence assignment significantly simplified. The good performance of this technique was shown by successful sequencing of the contents of several peptide maps. A similar approach was recently applied to nanoelectrospray ionization (nanoESI) and nano‐liquid chromatography/tandem mass spectrometry (LC/MS/MS). The MALDI‐TOF/TOF technique allows for fast, direct sequencing of modified peptides in proteomics samples, and is complementary to the nanoESI and nanoLC/MS/MS approaches. Copyright © 2006 John Wiley & Sons, Ltd.
ISSN:0951-4198
1097-0231
DOI:10.1002/rcm.2522