MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation
Peptide families are characterized by structural motifs, which often comprise specific post-translational modifications (PTMs) required for biological activity. In conventional bioactivity-based peptidomics studies natural peptide mixtures are chromatographically separated and the bioactive fraction...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2014-12-01
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| Series: | EuPA Open Proteomics |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2212968514000671 |
| _version_ | 1828861273168674816 |
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| author | Martijn Pinkse Geisa Evaristo Mervin Pieterse Yuanjie Yu Peter Verhaert |
| author_facet | Martijn Pinkse Geisa Evaristo Mervin Pieterse Yuanjie Yu Peter Verhaert |
| author_sort | Martijn Pinkse |
| collection | DOAJ |
| description | Peptide families are characterized by structural motifs, which often comprise specific post-translational modifications (PTMs) required for biological activity. In conventional bioactivity-based peptidomics studies natural peptide mixtures are chromatographically separated and the bioactive fractions purified to homogeneity, prior to structural characterization. In this paper we illustrate the reverse methodology, in which the primary structures of peptides with presumed bioactivity are first determined before investigating functions/bioactivities. We exemplify mass spectrometry (MS)-based strategies (employing, in particular, high resolution MS) to specifically select peptides – from complex mixtures such as frog defensive secretions – by virtue of the occurrence of particular PTMs, including amidation, disulfide-bonding, l- to d-amino acid isomerization, tyrosine-sulfation, proline-hydroxylation, and aminoterminal pyroglutamate formation. |
| first_indexed | 2024-12-13T02:58:01Z |
| format | Article |
| id | doaj.art-605b7d359f3c42bfbf40fe0305df8bad |
| institution | Directory Open Access Journal |
| issn | 2212-9685 |
| language | English |
| last_indexed | 2024-12-13T02:58:01Z |
| publishDate | 2014-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | EuPA Open Proteomics |
| spelling | doaj.art-605b7d359f3c42bfbf40fe0305df8bad2022-12-22T00:01:54ZengElsevierEuPA Open Proteomics2212-96852014-12-015C324010.1016/j.euprot.2014.11.001MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidationMartijn Pinkse0Geisa Evaristo1Mervin Pieterse2Yuanjie Yu3Peter Verhaert4Analytical Biotechnology and Innovative Peptide Biology Group, Department of Biotechnology, Delft University of Technology, Delft, The NetherlandsAnalytical Biotechnology and Innovative Peptide Biology Group, Department of Biotechnology, Delft University of Technology, Delft, The NetherlandsAnalytical Biotechnology and Innovative Peptide Biology Group, Department of Biotechnology, Delft University of Technology, Delft, The NetherlandsAnalytical Biotechnology and Innovative Peptide Biology Group, Department of Biotechnology, Delft University of Technology, Delft, The NetherlandsAnalytical Biotechnology and Innovative Peptide Biology Group, Department of Biotechnology, Delft University of Technology, Delft, The NetherlandsPeptide families are characterized by structural motifs, which often comprise specific post-translational modifications (PTMs) required for biological activity. In conventional bioactivity-based peptidomics studies natural peptide mixtures are chromatographically separated and the bioactive fractions purified to homogeneity, prior to structural characterization. In this paper we illustrate the reverse methodology, in which the primary structures of peptides with presumed bioactivity are first determined before investigating functions/bioactivities. We exemplify mass spectrometry (MS)-based strategies (employing, in particular, high resolution MS) to specifically select peptides – from complex mixtures such as frog defensive secretions – by virtue of the occurrence of particular PTMs, including amidation, disulfide-bonding, l- to d-amino acid isomerization, tyrosine-sulfation, proline-hydroxylation, and aminoterminal pyroglutamate formation.http://www.sciencedirect.com/science/article/pii/S2212968514000671Amphibian skin secretionAmidationd-Amino acidTyrosine-sulfationPyroglutamic acidDisulfide bridges |
| spellingShingle | Martijn Pinkse Geisa Evaristo Mervin Pieterse Yuanjie Yu Peter Verhaert MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation EuPA Open Proteomics Amphibian skin secretion Amidation d-Amino acid Tyrosine-sulfation Pyroglutamic acid Disulfide bridges |
| title | MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation |
| title_full | MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation |
| title_fullStr | MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation |
| title_full_unstemmed | MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation |
| title_short | MS approaches to select peptides with post-translational modifications from amphibian defense secretions prior to full sequence elucidation |
| title_sort | ms approaches to select peptides with post translational modifications from amphibian defense secretions prior to full sequence elucidation |
| topic | Amphibian skin secretion Amidation d-Amino acid Tyrosine-sulfation Pyroglutamic acid Disulfide bridges |
| url | http://www.sciencedirect.com/science/article/pii/S2212968514000671 |
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