The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry
Identifieur interne : 003112 ( Main/Exploration ); précédent : 003111; suivant : 003113The contributions of specific amino acid side chains to signal intensities of peptides in matrix‐assisted laser desorption/ionization mass spectrometry
Auteurs : Sabine Baumgart [Allemagne, États-Unis] ; Yvonne Lindner [Allemagne] ; Ronald Kühne [Allemagne] ; Axel Oberemm [Allemagne] ; Holger Wenschuh [Allemagne] ; Eberhard Krause [Allemagne]Source :
- Rapid Communications in Mass Spectrometry [ 0951-4198 ] ; 2004-04-30.
Abstract
Matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) analysis of complex peptide mixtures is often hampered by signal suppression effects as well as certain intrinsic properties of specific peptides that influence the desorption/ionization behavior. The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.
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DOI: 10.1002/rcm.1416
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The present systematic study reports on the relationship between the occurrence of certain amino acids in peptides and the intensities of the related ions which appear during MALDI‐MS analysis for both tryptic digests of proteins and synthetic peptide mixtures. The analysis of the tryptic digests revealed that the peptide sequences of the most intense peaks detected by MALDI‐MS contained significantly higher proportions of arginine, phenylalanine, proline, and leucine than the average values for the measured proteins. The relationship between the relative signal intensities and amino acid compositions of peptides was studied in more detail by the partial least squares (PLS) method using equimolar mixtures of 144 well‐characterized synthetic peptides. The regression coefficients clearly indicated that the presence of arginine, phenylalanine, leucine and proline tend to enhance the desorption/ionization process which results in higher MALDI‐MS peak intensities. Furthermore, it was shown that the impact of arginine depends strongly on the identity of adjacent amino acids. Copyright © 2004 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>Allemagne</li><li>États-Unis</li></country><region><li>Berlin</li><li>État de New York</li></region><settlement><li>Berlin</li><li>Ithaca (New York)</li></settlement><orgName><li>Université Cornell</li></orgName></list><tree><country name="Allemagne"><region name="Berlin"><name sortKey="Baumgart, Sabine" sort="Baumgart, Sabine" uniqKey="Baumgart S" first="Sabine" last="Baumgart">Sabine Baumgart</name></region><name sortKey="Krause, Eberhard" sort="Krause, Eberhard" uniqKey="Krause E" first="Eberhard" last="Krause">Eberhard Krause</name><name sortKey="Krause, Eberhard" sort="Krause, Eberhard" uniqKey="Krause E" first="Eberhard" last="Krause">Eberhard Krause</name><name sortKey="Krause, Eberhard" sort="Krause, Eberhard" uniqKey="Krause E" first="Eberhard" last="Krause">Eberhard Krause</name><name sortKey="Kuhne, Ronald" sort="Kuhne, Ronald" uniqKey="Kuhne R" first="Ronald" last="Kühne">Ronald Kühne</name><name sortKey="Lindner, Yvonne" sort="Lindner, Yvonne" uniqKey="Lindner Y" first="Yvonne" last="Lindner">Yvonne Lindner</name><name sortKey="Oberemm, Axel" sort="Oberemm, Axel" uniqKey="Oberemm A" first="Axel" last="Oberemm">Axel Oberemm</name><name sortKey="Wenschuh, Holger" sort="Wenschuh, Holger" uniqKey="Wenschuh H" first="Holger" last="Wenschuh">Holger Wenschuh</name></country><country name="États-Unis"><region name="État de New York"><name sortKey="Baumgart, Sabine" sort="Baumgart, Sabine" uniqKey="Baumgart S" first="Sabine" last="Baumgart">Sabine Baumgart</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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