ESI-MS/MS identification of a bradykinin-potentiating peptide from Amazon Bothrops atrox snake venom using a hybrid Qq-oaTOF mass spectrometer

A bradykinin-potentiating peptide (BPP) from Amazon Bothrops atrox venom with m/z 1384.7386 was identified and characterized by collision induced dissociation (CID) using an ESI-MS/MS spectra obtained in positive ion mode on a hybrid Qq-oaTOF mass spectrometer, Xevo G2 QTof MS (Waters, Manchester, U...

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Bibliographic Details
Published in:Toxins 2013-02, Vol.5 (2), p.327-335
Main Authors: Coutinho-Neto, Antonio, Caldeira, Cleópatra A S, Souza, Gustavo H M F, Zaqueo, Kayena D, Kayano, Anderson M, Silva, Rodrigo S, Zuliani, Juliana P, Soares, Andreimar M, Stábeli, Rodrigo G, Calderon, Leonardo A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
bioactive peptide
Bothrops
BPP
Bradykinin
Communication
Crotalid Venoms - chemistry
de novo peptide sequencing
Mass Spectrometry - methods
Oligopeptides - chemistry
Oligopeptides - isolation & purification
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
pyroglutamic acid
pyrrolidonecarboxylic acid
Sequence Alignment
Viper Venoms - chemistry
Viper Venoms - isolation & purification
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Summary:A bradykinin-potentiating peptide (BPP) from Amazon Bothrops atrox venom with m/z 1384.7386 was identified and characterized by collision induced dissociation (CID) using an ESI-MS/MS spectra obtained in positive ion mode on a hybrid Qq-oaTOF mass spectrometer, Xevo G2 QTof MS (Waters, Manchester, UK). De novo peptide sequence analysis of the CID fragmentation spectra showed the amino acid sequence ZKWPRPGPEIPP, with a pyroglutamic acid and theoretical monoisotopic m/z 1384.7378, which is similar to experimental data, showing a mass accuracy of 0.6 ppm. The peptide is homologous to other BPP from Bothrops moojeni and was named as BPP-BAX12.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins5020327