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Fucase TM, Sciani JM, Cavalcante I, et al. Isolation and biochemical characterization of bradykinin-potentiating peptides from . J Venom Anim Toxins Incl Trop Dis. 2017;23:33doi: 10.1186/s40409-017-0124-9.
Fucase, T. M., Sciani, J. M., Cavalcante, I., Viala, V. L., Chagas, B. B., Pimenta, D. C., & Spencer, P. J. (2017). Isolation and biochemical characterization of bradykinin-potentiating peptides from . The journal of venomous animals and toxins including tropical diseases, 2333. https://doi.org/10.1186/s40409-017-0124-9
Fucase, Tamara M, et al. "Isolation and biochemical characterization of bradykinin-potentiating peptides from ." The journal of venomous animals and toxins including tropical diseases vol. 23 (2017): 33. doi: https://doi.org/10.1186/s40409-017-0124-9
Fucase TM, Sciani JM, Cavalcante I, Viala VL, Chagas BB, Pimenta DC, Spencer PJ. Isolation and biochemical characterization of bradykinin-potentiating peptides from . J Venom Anim Toxins Incl Trop Dis. 2017 Jun 26;23:33. doi: 10.1186/s40409-017-0124-9. eCollection 2017. PMID: 28670326; PMCID: PMC5485657.
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J Venom Anim Toxins Incl Trop Dis. 2017 Jun 26;23:33. doi: 10.1186/s40409-017-0124-9. eCollection 2017.

Isolation and biochemical characterization of bradykinin-potentiating peptides from .

The journal of venomous animals and toxins including tropical diseases

Tamara M Fucase, Juliana M Sciani, Ingrid Cavalcante, Vincent L Viala, Bruno B Chagas, Daniel C Pimenta, Patrick J Spencer

Affiliations

  1. Biotechnology Center, Nuclear and Energy Research Institute (IPEN), Av. Lineu Prestes, 2242, São Paulo, SP CEP 05508-000 Brazil.
  2. Laboratory of Biochemistry and Biophysics, Butantan Institute, Av. Vital Brasil, 1500, São Paulo, SP CEP 05503-900 Brazil.

PMID: 28670326 PMCID: PMC5485657 DOI: 10.1186/s40409-017-0124-9

Abstract

BACKGROUND: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13 residues with a high number of proline residues and the tripeptide Ile-Pro-Pro (IPP-tripeptide) in the C-terminus region and have a conserved N-terminal pyroglutamate residue. As a whole, the action of the BPPs on prey and snakebite victims results in the decrease of the blood pressure. The aim of this work was to isolate and characterize novel BPPs from the venom of

METHODS: The crude venom of

RESULTS: Typical BPP signatures were identified in three RP-HPLC fractions. CID fragmentation presented the usual y-ion of the terminal P-P fragment as a predominant signal at m/z 213.1.

CONCLUSIONS: So far, few BPPs are described in Viperinae, and based on the sequenced peptides, two non-canonical sequences were detected. The possible clinical role of this new peptides remains unclear.

Keywords: Hypotension; Peptide; Viperinae

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