De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
EU-Projektnummer
DFG-Projektnummer
Projekt
Open Access-Veröffentlichung
Sammlungen
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
unikn.publication.listelement.citation.prefix.version.undefined
Zusammenfassung
An efficient approach in combinatorial chemistry is the synthesis of one-bead-one-compound peptide libraries. In contrast to synthesis and functional screening, which is performed in a largely automated manner, structure determination has been frequently laborious and time-consuming. Here we report an approach for de novo sequencing of peptides on single beads by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance (MALDI-FTICR) tandem mass spectrometry, using a resin with a photolinker for solid-phase peptide synthesis. Upon sorting out single beads, an efficient sample preparation on the MALDI target was developed that enables fragmentation upon irradiation of the bead-matrix mixture with the ultraviolet (UV)-MALDI laser, with enhanced yield of sequence-specific fragment ions at increased laser energy. This approach is illustrated by sequence determinations of two peptides from a library with sequences varying in a single amino acid; the feasibility with tandem-MS procedures and fragment ion assignment was ascertained by sustained off-resonance irradiation/collision induced dissociation (SORI/CID) and infrared multiphoton dissociation (IRMPD) fragmentation.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
SEMMLER, Angelika, Reinhold WEBER, Michael PRZYBYLSKI, Valentin WITTMANN, 2010. De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry. In: Journal of the American Society for Mass Spectrometry. 2010, 21(2), pp. 215-219. ISSN 1044-0305. eISSN 1879-1123. Available under: doi: 10.1016/j.jasms.2009.10.004BibTex
@article{Semmler2010seque-9644, year={2010}, doi={10.1016/j.jasms.2009.10.004}, title={De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry}, number={2}, volume={21}, issn={1044-0305}, journal={Journal of the American Society for Mass Spectrometry}, pages={215--219}, author={Semmler, Angelika and Weber, Reinhold and Przybylski, Michael and Wittmann, Valentin} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/9644"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:13:24Z</dc:date> <dc:creator>Przybylski, Michael</dc:creator> <dc:contributor>Przybylski, Michael</dc:contributor> <dc:contributor>Semmler, Angelika</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/9644"/> <dc:language>eng</dc:language> <dcterms:issued>2010</dcterms:issued> <dc:format>application/pdf</dc:format> <dc:contributor>Weber, Reinhold</dc:contributor> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <dc:rights>terms-of-use</dc:rights> <dcterms:bibliographicCitation>First publ. in: Journal of the American Society for Mass Spectrometry ; 21 (2010), 2. - S. 215-219</dcterms:bibliographicCitation> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9644/1/Przybylski_Michael2009_k.pdf"/> <dc:creator>Wittmann, Valentin</dc:creator> <dc:contributor>Wittmann, Valentin</dc:contributor> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/9644/1/Przybylski_Michael2009_k.pdf"/> <dcterms:title>De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry</dcterms:title> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Semmler, Angelika</dc:creator> <dc:creator>Weber, Reinhold</dc:creator> <dcterms:abstract xml:lang="eng">An efficient approach in combinatorial chemistry is the synthesis of one-bead-one-compound peptide libraries. In contrast to synthesis and functional screening, which is performed in a largely automated manner, structure determination has been frequently laborious and time-consuming. Here we report an approach for de novo sequencing of peptides on single beads by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance (MALDI-FTICR) tandem mass spectrometry, using a resin with a photolinker for solid-phase peptide synthesis. Upon sorting out single beads, an efficient sample preparation on the MALDI target was developed that enables fragmentation upon irradiation of the bead-matrix mixture with the ultraviolet (UV)-MALDI laser, with enhanced yield of sequence-specific fragment ions at increased laser energy. This approach is illustrated by sequence determinations of two peptides from a library with sequences varying in a single amino acid; the feasibility with tandem-MS procedures and fragment ion assignment was ascertained by sustained off-resonance irradiation/collision induced dissociation (SORI/CID) and infrared multiphoton dissociation (IRMPD) fragmentation.</dcterms:abstract> </rdf:Description> </rdf:RDF>