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Reply to the Letter "Create Guidelines for Characterization of Venom Peptides" from Dr. Volker Herzig.

ABSTRACT: Regarding our paper "PhTx3-4, a Spider Toxin Calcium Channel Blocker, Reduces NMDA-Induced Injury of the Retina", published in Toxins 2016, 8, doi:10.3390/toxins8030070 [1].[...].

SUBMITTER: Gomez MV

PROVIDER: S-EPMC5037479 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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Reply to the Letter "Create Guidelines for Characterization of Venom Peptides" from Dr. Volker Herzig.

Gomez Marcus Vinicius MV

Toxins 20160830 9

Regarding our paper "PhTx3-4, a Spider Toxin Calcium Channel Blocker, Reduces NMDA-Induced Injury of the Retina", published in Toxins 2016, 8, doi:10.3390/toxins8030070 [1].[...]. ...[more]

PMID: 27589796

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Project description:BACKGROUND:Snake 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. RESULTS:The 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 ?M. The IC50 value of the peptide ZQWAQGRAPHPP was 3.63 ?M. CONCLUSION:The 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.

Dataset Information

Reply to the Letter "Create Guidelines for Characterization of Venom Peptides" from Dr. Volker Herzig.

Publications

Reply to the Letter "Create Guidelines for Characterization of Venom Peptides" from Dr. Volker Herzig.

Similar Datasets

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