Bradykinin-Potentiating Peptides (BPP)

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CAT# Product Name M.W Molecular Formula Inquiry
B08001 BPP-14a Inquiry
B08002 BPP-11a Inquiry
B08003 BPP-12c Inquiry
B08004 BPP-11a-F Inquiry
B08005 BPP-5b Inquiry
B08006 BPP-9a Inquiry
B08007 BPP-9aF Inquiry
B08008 BPP-10b Inquiry
B08009 A-VI-5 548.59 Inquiry
B08010 BPP 5a 611.7 C₃₀H₄₁N₇O₇ Inquiry
B08011 BPP 9a 1101.27 C53H76N14O12 Inquiry
B08012 [Des-Arg10]-HOE I40 Inquiry
B08013 HOE I40 Inquiry
C40001 Contraction-inhibiting peptide 1 Inquiry
C40002 Contraction-inhibiting peptide 2 Inquiry
C40003 Blomhotin Inquiry
C40004 Bradykinin-potentiating peptide Ahb2 Inquiry
C40005 Bradykinin-potentiating peptide Ahb1 Inquiry
C40006 Bradykinin-potentiating peptide E Inquiry
C40007 Bradykinin-potentiating peptide B Inquiry

Introduction

Bradykinin-potentiating peptides are proline-rich peptides known to inhibit angiotensin-converting enzyme (ACE). This enzyme is responsible for the conversion of angiotensin I to angiotensin II. Angiotensin II is an effective vasoconstrictor and hypertension agent. The first bradykinin-potentiating peptide was discovered by Ferreira and Rocha e Silva and termed as such due to its pharmacological effect, i.e., literally potentiate/enhance the effect of bradykinin (BK), in comparison to the same BK dose administered prior to the bradykinin-potentiating peptide treatment, without presenting any hypotensive effect. Since then, bio-driven assays have found several bradykinin-potentiating peptides from many sources, such as scorpion venom, tree frog skin secretions, and snake venom from other species. Snake bradykinin-potentiating peptides are mostly less than 14-mer proline-rich peptides, presenting three distinct features. The first one is an almost invariable pyroglutamic acid at the N-terminus. The second is the presence of a Pro residue at the C-terminus for peptides containing up to five residues The third is the presence of the tripeptide Ile-Pro-Pro at the C-terminus of less than 5-mer peptides containing up to 14 residues.

Mechanism of action

Bradykinin-potentiating peptides’ biological properties are associated with impairment of angiotensin II generation and bradykinin degradation. By inhibiting ACE, BPPs inhibit the formation of angiotensin II and lower blood pressure. In addition, since this enzyme is also capable of cleaving bradykinin, a hypotensive peptide, its inhibition involves two different mechanism targets (angiotensin and bradykinin), causing a comprehensive antihypertensive effect. After administration, the global physiological effect of the bradykinin-potentiating peptide is the decrease of the blood pressure.

Application of Bradykinin-Potentiating Peptides

Because of the interesting effect of bradykinin-potentiating peptides, David Cushman et al use one of these peptides to develop blood pressure lowering drugs, and the well-known captopril is widely used in the treatment of hypertension. From that time on, many studies on bradykinin-potentiating peptides have been conducted, basically describing new peptides and assaying their pharmacological effects, mostly in comparison to captopril. Therefore, Bradykinin-potentiating Peptides will be an ideal treatment for high blood pressure.

Reference

  1. Habermehl, G.G., M?llring, Th., Coelfen, A., Ferreira, L.A.F. (1995). Bradykinin-potentiating peptides in snake venoms. Toxicon, 33(3), 257-258.
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