Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
High‐sensitivity, rapid identification of proteins in proteomic studies normally uses a combination of one‐ or two‐dimensional electrophoresis together with mass spectrometry. The simplicity and sensitivity of matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS)...
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| Published in | Journal of mass spectrometry. Vol. 38; no. 4; pp. 373 - 377 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.04.2003
Wiley |
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| Online Access | Get full text |
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| Abstract | High‐sensitivity, rapid identification of proteins in proteomic studies normally uses a combination of one‐ or two‐dimensional electrophoresis together with mass spectrometry. The simplicity and sensitivity of matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) have increased its application in recent years. The most common method of ‘peptide fingerprinting’ often may not provide robust identification. Normally additional sequence information by post‐source decay (PSD) MALDI‐TOFMS provides additional constraints for database searches to achieve highly confident results. Here we describe a derivatization procedure to facilitate the acquisition of such sequence information. Peptide digests from a skin‐expressed protein were modified with 4‐sulfophenyl isothiocyanate. The resulting peptides carry a fixed negative charge at the N‐terminal end and the resulting PSD spectrum is dominated by C‐terminal y‐type ions. The sequence information in most cases can be obtained manually or with simple programming tools. Methods of optimizing the procedure and increasing the sensitivity are discussed. Copyright © 2003 John Wiley & Sons, Ltd. |
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| AbstractList | High-sensitivity, rapid identification of proteins in proteomic studies normally uses a combination of one- or two-dimensional electrophoresis together with mass spectrometry. The simplicity and sensitivity of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) have increased its application in recent years. The most common method of 'peptide fingerprinting' often may not provide robust identification. Normally additional sequence information by post-source decay (PSD) MALDI-TOFMS provides additional constraints for database searches to achieve highly confident results. Here we describe a derivatization procedure to facilitate the acquisition of such sequence information. Peptide digests from a skin-expressed protein were modified with 4-sulfophenyl isothiocyanate. The resulting peptides carry a fixed negative charge at the N-terminal end and the resulting PSD spectrum is dominated by C-terminal y-type ions. The sequence information in most cases can be obtained manually or with simple programming tools. Methods of optimizing the procedure and increasing the sensitivity are discussed. High‐sensitivity, rapid identification of proteins in proteomic studies normally uses a combination of one‐ or two‐dimensional electrophoresis together with mass spectrometry. The simplicity and sensitivity of matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) have increased its application in recent years. The most common method of ‘peptide fingerprinting’ often may not provide robust identification. Normally additional sequence information by post‐source decay (PSD) MALDI‐TOFMS provides additional constraints for database searches to achieve highly confident results. Here we describe a derivatization procedure to facilitate the acquisition of such sequence information. Peptide digests from a skin‐expressed protein were modified with 4‐sulfophenyl isothiocyanate. The resulting peptides carry a fixed negative charge at the N‐terminal end and the resulting PSD spectrum is dominated by C‐terminal y‐type ions. The sequence information in most cases can be obtained manually or with simple programming tools. Methods of optimizing the procedure and increasing the sensitivity are discussed. Copyright © 2003 John Wiley & Sons, Ltd. |
| Author | Marekov, Lyuben N. Steinert, Peter M. |
| Author_xml | – sequence: 1 givenname: Lyuben N. surname: Marekov fullname: Marekov, Lyuben N. email: marekovl@mail.nih.gov organization: Laboratory of Skin Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA – sequence: 2 givenname: Peter M. surname: Steinert fullname: Steinert, Peter M. organization: Laboratory of Skin Biology, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA |
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| Keywords | charge derivatization peptides Matrix assisted laser desorption ionization Derivatization Sulfonic acid Protein Binding protein Time of flight method Organic isothiocyanate matrix-assisted laser desorption/ionization time-of-flight mass spectrometry post-source decay Mass spectrometry Sequencing Calmodulin Structural analysis |
| Language | English |
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| SubjectTerms | Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Benzenesulfonates - chemistry Biological and medical sciences Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - metabolism charge derivatization Fundamental and applied biological sciences. Psychology Humans Isothiocyanates - chemistry matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Molecular Sequence Data Peptide Fragments - chemistry peptides post-source decay Proteins Sequence Analysis, Protein sequencing Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Transglutaminases - chemistry Transglutaminases - metabolism Trypsin - metabolism |
| Title | Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry |
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