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Tityus serrulatus venom peptidomics: Assessing venom peptide diversity
- Source :
- Toxicon. 52:611-618
- Publication Year :
- 2008
- Publisher :
- Elsevier BV, 2008.
-
Abstract
- MALDI-TOF-TOF and de novo sequencing were employed to assess the Tityus serrulatus venom peptide diversity. Previous works has shown the cornucopia of molecular masses, ranging from 800 to 3000Da, present in the venom from this and other scorpions species. This work reports the identification/sequencing of several of these peptides. The majority of the peptides found were fragments of larger venom toxins. For instance, 28 peptides could be identified as fragments from Pape proteins, 10 peptides corresponded to N-terminal fragments of the TsK beta (scorpine-like) toxin and fragments of potassium channel toxins (other than the k-beta) were sequenced as well. N-terminal fragments from the T. serrulatus hypotensins-I and II and a novel hypotensin-like peptide could also be found. This work also reports the sequencing of novel peptides without sequence similarities to other known molecules.
- Subjects :
- Tityus serrulatus
Molecular Sequence Data
Scorpion Venoms
Venom
Peptide
Chemical Fractionation
Toxicology
medicine.disease_cause
Animal origin
Sequence Analysis, Protein
Tandem Mass Spectrometry
medicine
Animals
De novo sequencing
Amino Acid Sequence
chemistry.chemical_classification
biology
Toxin
Anatomy
biology.organism_classification
chemistry
Biochemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chromatography, Gel
Peptides
Sequence Alignment
Subjects
Details
- ISSN :
- 00410101
- Volume :
- 52
- Database :
- OpenAIRE
- Journal :
- Toxicon
- Accession number :
- edsair.doi.dedup.....7fae3933162597aa8040344108130cb2
- Full Text :
- https://doi.org/10.1016/j.toxicon.2008.07.010