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

Autor: Coutinho-Neto A; Center of Biomolecules Study Applied to Health, Fiocruz Rondônia, Oswaldo Cruz Foundation, Porto Velho, RO, Brazil. antonio.dnabrasil@gmail.com, Caldeira CA, Souza GH, Zaqueo KD, Kayano AM, Silva RS, Zuliani JP, Soares AM, Stábeli RG, Calderon LA
Jazyk: angličtina
Zdroj: Toxins [Toxins (Basel)] 2013 Feb 18; Vol. 5 (2), pp. 327-35. Date of Electronic Publication: 2013 Feb 18.
DOI: 10.3390/toxins5020327
Abstrakt: 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.
Databáze: MEDLINE