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Status: Bibliographieeintrag
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Verfasst von:Oosten, Luuk N. van [VerfasserIn]   i
 Pinkse, Martijn W. H. [VerfasserIn]   i
 Pieterse, Mervin [VerfasserIn]   i
 Escoubas, Pierre [VerfasserIn]   i
 Verhaert, Peter D. E. M. [VerfasserIn]   i
Titel:High-accuracy mass spectrometry based screening method for the discovery of cysteine containing peptides in animal venoms and toxins
Verf.angabe:Luuk N. van Oosten, Martijn W.H. Pinkse, Mervin Pieterse, Pierre Escoubas, Peter D.E.M. Verhaert
E-Jahr:2018
Jahr:24 February 2018
Umfang:14 S.
Fussnoten:Gesehen am 20.03.2020
Titel Quelle:Enthalten in: Peptidomics
Ort Quelle:New York, NY : Humana Press, 2018
Jahr Quelle:2018
Band/Heft Quelle:(2018), Seite 335-348
ISBN Quelle:978-1-4939-7537-2
Abstract:Venom and toxin samples derived from animal origins are a rich source of bioactive peptides. A high proportion of bioactive peptides that have been identified in venom contain one or more disulfide bridges, which are thought to stabilize tertiary structure, and therefore influence the peptides' specificity and activity. In this chapter, we describe a label-free mass spectrometry-based screening workflow specifically to detect peptides that contain inter- and intramolecular disulfide bonds, followed by elucidation of their primary structure. This method is based on the determination of the normalized isotope shift (NIS) and the normalized mass defect (NMD) of peptides, two parameters which are heavily influenced by the presence of sulfur in a peptide, where cysteines are the main contributing residues. Using ant defensive secretions as an example, we describe the initial fractionation of the venom on strong cation exchange followed by nanoflow HPLC and mass spectrometry. High resolution zoom scan spectra of high-abundance peptides are acquired, allowing an accurate determination of both monoisotopic and average mass, which are essential for calculation of NMD and NIS. Candidate peptides exhibiting relative low NMD and high NIS values are selected for targeted de novo sequencing. By fine-tuning the collision energy for optimal fragmentation of each selected precursor ions, the full sequence of several novel inter- and intramolecular disulfide bond containing ant defensive peptides can be established.
DOI:doi:10.1007/978-1-4939-7537-2_22
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1007/978-1-4939-7537-2_22
 DOI: https://doi.org/10.1007/978-1-4939-7537-2_22
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Animals
 Ants
 Cysteine
 De novo sequencing
 Disulfide bridge
 High-Throughput Screening Assays
 Isotope shift
 Mass defect
 Mass Spectrometry
 Orbitrap
 Peptide
 Peptide Fragments
 Toxin
 Toxins, Biological
 Venom
 Venoms
K10plus-PPN:169303803X
Verknüpfungen:→ Sammelwerk

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