Dataset Information

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A₂ Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization.

ABSTRACT: This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A₂ (PLA₂) from Agkistrodon contortrix pictigaster venom. Both PLA₂s were highly purified by a single chromatographic step on a C₁₈ reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA₂ toxins from viperid snake venoms. ACP-TX-I belongs to the catalytically inactive K49 PLA₂ class, while ACP-TX-II is a D49 PLA₂, and is enzymatically active. ACP-TX-I PLA₂ is monomeric, which results in markedly diminished myotoxic and inflammatory activities when compared with dimeric K49 PLA₂s, confirming the hypothesis that dimeric structure contributes heavily to the profound myotoxicity of the most active viperid K49 PLA₂s. ACP-TX-II exhibits the main pharmacological actions reported for this protein family, including in vivo local myotoxicity, edema-forming activity, and in vitro cytotoxicity. ACP-TX-I PLA₂ is cytotoxic to A549 lung carcinoma cells, indicating that cytotoxicity to these tumor cells does not require enzymatic activity.

SUBMITTER: Huancahuire-Vega S

PROVIDER: S-EPMC6891687 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Publications

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A2 Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization.

Huancahuire-Vega Salomón S Hollanda Luciana M LM Gomes-Heleno Mauricio M Newball-Noriega Edda E EE Marangoni Sergio S

Toxins 20191114 11

This work reports the purification and biochemical and functional characterization of ACP-TX-I and ACP-TX-II, two phospholipases A2 (PLA2) from Agkistrodon contortrix pictigaster venom. Both PLA2s were highly purified by a single chromatographic step on a C18 reverse phase HPLC column. Various peptide sequences from these two toxins showed similarity to those of other PLA2 toxins from viperid snake venoms. ACP-TX-I belongs to the cata ...[more]

PMID: 31739403

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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

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A₂ Isolated from Trans-Pecos Copperhead Agkistrodon contortrix pictigaster Venom: Biochemical and Functional Characterization.

Publications

ACP-TX-I and ACP-TX-II, Two Novel Phospholipases A<sub>2</sub> Isolated from Trans-Pecos Copperhead <i>Agkistrodon contortrix pictigaster</i> Venom: Biochemical and Functional Characterization.

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