ESI-MS/MS Identification of a Bradykinin-Potentiating Peptide from Amazon Bothrops atrox Snake Venom Using a Hybrid Qq-oaTOF Mass Spectrometer

Toxins

Antonio Coutinho-Neto²  Cleópatra A. S. Caldeira²  Gustavo H. M. F. Souza¹  Kayena D. Zaqueo²  Anderson M. Kayano²  Rodrigo S. Silva²  Juliana P. Zuliani²  Andreimar M. Soares²  Rodrigo G. Stli² 

[1]MS Applications Development Laboratory, Waters Corporation, Alphaville, SP 06455-020, Brazil

[2] E-Mail:

[3]Center of Biomolecules Study Applied to Health, Fiocruz Rondônia, Oswaldo Cruz Foundation, Porto Velho, RO 76820-245, Brazil

[4] E-Mails:

关键词: bioactive peptide;    BPP;    pyroglutamic acid;    pyrrolidonecarboxylic acid;    de novo peptide sequencing;   

DOI  :  10.3390/toxins5020327

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.