ArticleProteome science2016
Isolation and characterization of Bradykinin potentiating peptides from Agkistrodon bilineatus venom.
Article in Proteome science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular Recognition and Immunopharmacological Implications of Serratiopeptidase Targeting Snake Venom Bradykinin-Potentiating Peptides.Pharmaceutical research · 2026Article
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- Intraspecific Differences in the Venom ofToxins · 2022Article
- Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases.Molecules (Basel, Switzerland) · 2021Review
- Snake venom-derived bradykinin-potentiating peptides: A promising therapy for COVID-19?Drug development research · 2021Review
- Antivenomics and in vivo preclinical efficacy of six Latin American antivenoms towards south-western Colombian Bothrops asper lineage venoms.PLoS neglected tropical diseases · 2021Article
- Proteomic Investigations of Two PakistaniToxins · 2020Article
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- Hypotensive Snake Venom Components-A Mini-Review.Molecules (Basel, Switzerland) · 2019Review
- Snake Venom Peptides: Tools of Biodiscovery.Toxins · 2018Review
- Snake Venom Extracellular vesicles (SVEVs) reveal wide molecular and functional proteome diversity.Scientific reports · 2018Article
- Rapid screening and identification of ACE inhibitors in snake venoms using at-line nanofractionation LC-MS.Analytical and bioanalytical chemistry · 2017Article
- Isolation and biochemical characterization of bradykinin-potentiating peptides fromThe journal of venomous animals and toxins including tropical diseases · 2017Article
- Proteomic Analyses of Agkistrodon contortrix contortrix Venom Using 2D Electrophoresis and MS Techniques.Toxins · 2016Article
- Proteome and Peptidome of Vipera berus berus Venom.Molecules (Basel, Switzerland) · 2016Article
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSnake venom is a source of many pharmacologically important molecules. Agkistrodon bilineatus commonly known as Cantil, is spread over Central America particularly in Mexico and Costa Rica. From the venom of Agkistrodon bilineatus we have isolated and characterised six hypotensive peptides, and two bradykinin inhibitor peptides. The IC-50 value of four synthesized peptides was studied, towards angiotensin converting enzyme, in order to study the structure-function relationship of these peptides.
resultsThe purification of the peptides was carried out by size exclusion chromatography, followed by reverse phase chromatography. Sequences of all peptides were determined applying MALDI-TOF/TOF mass spectrometry. These hypotensive peptides bear homology to bradykinin potentiating peptides and venom vasodilator peptide. The peptide with m/z 1355.53 (M + H)(+1), and the corresponding sequence ZQWAQGRAPHPP, we identified for the first time. A precursor protein containing a fragment of this peptide was reported at genome level, (Uniprot ID P68515), in Bothrops insularis venom gland. These proline rich hypotensive peptides or bradykinin potentiating peptides are usually present in the venom of Crotalinae, and exhibit specificity in binding to the C domain of somatic angiotensin converting enzyme. Four of these hypotensive peptides, were selected and synthesized to obtain the required quantity to study their IC50 values in complex with the angiotensin converting enzyme. The peptide with the sequence ZLWPRPQIPP displayed the lowest IC50 value of 0.64 μM. The IC50 value of the peptide ZQWAQGRAPHPP was 3.63 μM.
conclusionThe canonical snake venom BPPs classically display the IPP motif at the C-terminus. Our data suggest that the replacement of the highly conserved hydrophobic isoleucine by histidine does not affect the inhibitory activity, indicating that isoleucine is not mandatory to inhibit the angiotensin converting enzyme. The evaluation of IC 50 values show that the peptide with basic pI value exhibits a lower IC 50 value.
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