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Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels.
Toxicon. 2008 Aug 01; 52(2):228-36.T

Abstract

Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker omega-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides.

Authors+Show Affiliations

Centro de Investigación en Biotecnología - UAEM, Av. Universidad 2001, Cuernavaca, Morelos 62210, México. elbav@buzon.uaem.mxNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18606178

Citation

Villegas, Elba, et al. "Biochemical Characterization of Cysteine-rich Peptides From Oxyopes Sp. Venom That Block Calcium Ion Channels." Toxicon : Official Journal of the International Society On Toxinology, vol. 52, no. 2, 2008, pp. 228-36.
Villegas E, Adachi-Akahane S, Bosmans F, et al. Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels. Toxicon. 2008;52(2):228-36.
Villegas, E., Adachi-Akahane, S., Bosmans, F., Tytgat, J., Nakajima, T., & Corzo, G. (2008). Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels. Toxicon : Official Journal of the International Society On Toxinology, 52(2), 228-36. https://doi.org/10.1016/j.toxicon.2008.05.019
Villegas E, et al. Biochemical Characterization of Cysteine-rich Peptides From Oxyopes Sp. Venom That Block Calcium Ion Channels. Toxicon. 2008 Aug 1;52(2):228-36. PubMed PMID: 18606178.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical characterization of cysteine-rich peptides from Oxyopes sp. venom that block calcium ion channels. AU - Villegas,Elba, AU - Adachi-Akahane,Satomi, AU - Bosmans,Frank, AU - Tytgat,Jan, AU - Nakajima,Terumi, AU - Corzo,Gerardo, Y1 - 2008/06/11/ PY - 2008/02/06/received PY - 2008/04/01/revised PY - 2008/05/01/accepted PY - 2008/7/9/pubmed PY - 2008/10/29/medline PY - 2008/7/9/entrez SP - 228 EP - 36 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 52 IS - 2 N2 - Oxytoxins (OxyTx1 and OxyTx2) are disulfide-rich peptides isolated from the venom of the spider Oxyopes lineatus that block voltage-sensitive calcium ion channels (VSCCs). OxyTx1 was identified previously and isolated from the related spider Oxyopes kitabensis; however, its pharmacology was unknown. OxyTx1 and OxyTx2 contain 69 and 55 amino acid residues with molecular masses of 8058.2 and 6175.2Da, respectively. Oxytoxins contain five disulfide bridges, are amidated at their C-terminus, antagonize P/Q-, N- or L-type VSCCs, and have low amino acid identity to known VSCC blockers from arthropod venoms. OxyTx1 is not specific for VSCCs subtypes when compared to the classical P/Q-type blocker omega-AgaIVA, but OxyTx1 has higher paralytic activity towards Spodoptera litura larvae. Because of their structural and biochemical characteristics OxyTx1 and OxyTx2 may represent a new family of insecticidal peptides. SN - 0041-0101 UR - https://www.unboundmedicine.com/medline/citation/18606178/Biochemical_characterization_of_cysteine_rich_peptides_from_Oxyopes_sp__venom_that_block_calcium_ion_channels_ L2 - http://ovidsp.ovid.com/ovidweb.cgi?T=JS&PAGE=linkout&SEARCH=18606178.ui DB - PRIME DP - Unbound Medicine ER -