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Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2.
Biochim Biophys Acta. 2009 Aug; 1794(8):1190-6.BB

Abstract

Soluble venom and purified fractions of the theraposid spider Brachypelma albiceps were screened for insecticidal peptides based on toxicity to crickets. Two insecticidal peptides, named Ba1 and Ba2, were obtained after the soluble venom was separated by high performance liquid chromatography and cation exchange chromatography. The two insecticidal peptides contain 39 amino acid residues and three disulfide bonds, and based on their amino acid sequence, they are highly identical to the insecticidal peptides from the theraposid spiders Aphonopelma sp. from the USA and Haplopelma huwenum from China indicating a relationship among these genera. Although Ba1 and Ba2 were not able to modify currents in insect and vertebrate cloned voltage-gated sodium ion channels, they have noteworthy insecticidal activities compared to classical arachnid insecticidal toxins indicating that they might target unknown receptors in insect species. The most abundant insecticidal peptide Ba2 was submitted to NMR spectroscopy to determine its 3-D structure; a remarkable characteristic of Ba2 is a cluster of basic residues, which might be important for receptor recognition.

Authors+Show Affiliations

Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, UNAM, Cuernavaca, Morelos, Mexico. corzo@ibt.unam.mxNo affiliation info availableNo affiliation info availableNo affiliation info availableNo 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

19374957

Citation

Corzo, Gerardo, et al. "Insecticidal Peptides From the Theraposid Spider Brachypelma Albiceps: an NMR-based Model of Ba2." Biochimica Et Biophysica Acta, vol. 1794, no. 8, 2009, pp. 1190-6.
Corzo G, Bernard C, Clement H, et al. Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2. Biochim Biophys Acta. 2009;1794(8):1190-6.
Corzo, G., Bernard, C., Clement, H., Villegas, E., Bosmans, F., Tytgat, J., Possani, L. D., Darbon, H., & Alagón, A. (2009). Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2. Biochimica Et Biophysica Acta, 1794(8), 1190-6. https://doi.org/10.1016/j.bbapap.2009.04.004
Corzo G, et al. Insecticidal Peptides From the Theraposid Spider Brachypelma Albiceps: an NMR-based Model of Ba2. Biochim Biophys Acta. 2009;1794(8):1190-6. PubMed PMID: 19374957.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Insecticidal peptides from the theraposid spider Brachypelma albiceps: an NMR-based model of Ba2. AU - Corzo,Gerardo, AU - Bernard,Cedric, AU - Clement,Herlinda, AU - Villegas,Elba, AU - Bosmans,Frank, AU - Tytgat,Jan, AU - Possani,Lourival D, AU - Darbon,Herve, AU - Alagón,Alejandro, Y1 - 2009/04/15/ PY - 2009/01/08/received PY - 2009/04/01/revised PY - 2009/04/06/accepted PY - 2009/4/21/entrez PY - 2009/4/21/pubmed PY - 2009/9/2/medline SP - 1190 EP - 6 JF - Biochimica et biophysica acta JO - Biochim. Biophys. Acta VL - 1794 IS - 8 N2 - Soluble venom and purified fractions of the theraposid spider Brachypelma albiceps were screened for insecticidal peptides based on toxicity to crickets. Two insecticidal peptides, named Ba1 and Ba2, were obtained after the soluble venom was separated by high performance liquid chromatography and cation exchange chromatography. The two insecticidal peptides contain 39 amino acid residues and three disulfide bonds, and based on their amino acid sequence, they are highly identical to the insecticidal peptides from the theraposid spiders Aphonopelma sp. from the USA and Haplopelma huwenum from China indicating a relationship among these genera. Although Ba1 and Ba2 were not able to modify currents in insect and vertebrate cloned voltage-gated sodium ion channels, they have noteworthy insecticidal activities compared to classical arachnid insecticidal toxins indicating that they might target unknown receptors in insect species. The most abundant insecticidal peptide Ba2 was submitted to NMR spectroscopy to determine its 3-D structure; a remarkable characteristic of Ba2 is a cluster of basic residues, which might be important for receptor recognition. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/19374957/Insecticidal_peptides_from_the_theraposid_spider_Brachypelma_albiceps:_an_NMR_based_model_of_Ba2_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1570-9639(09)00094-6 DB - PRIME DP - Unbound Medicine ER -