Pi5 and Pi6, two undescribed peptides from the venom of the scorpion Pandinus imperator and their effects on K+-channels


Por: Olamendi-Portugal, T., Csoti, A., Jimenez-Vargas, J. M., Gomez-Lagunas, F., Panyi, G., Possani, L. D.

Publicada: 1 jul 2017
Categoría: Toxicology

Resumen:
This work reports the isolation, chemical and functional characterization of two previously unknown peptides purified from the venom of the scorpion Pandinus imperator, denominated Pi5 and Pi6. Pi5 is a classical K+-channel blocking peptide containing 33 amino acid residues with 4 disulfide bonds. It is the first member of a new subfamily, here defined by the systematic number alpha-KTx 24.1. Pi6 is a peptide of unknown real function, containing only two disulfide bonds and 28 amino acid residues, but showing sequence similarities to the kappa-family of K-channel toxins. The systematic number assigned is kappa-KTx2.9. The function of both peptides was assayed on Drosophila Shab and Shaker K+-channels, as well as four different subtypes of voltage-dependent K+-channels: hKv1.1, hKv1.2, hKv1.3 and hKv1.4. The electro-physiological assays showed that Pi5 inhibited Shaker B, hKv1.1, hKv1.2 and hKv1.3 channels with Kd = 540 nM, KD = 92 nM and Kd = 77 nM, respectively, other studied channels were not affected. Of the channels tested only hKv1.2 and hKv1.3 were inhibited at 100 nM concentration of Pi6, the remaining current fractions were 68% and 77%, respectively. Thus, Pi5 and Pi6 are high nanomolar affinity nonselective blockers of hKv1.2 and hKv1.3 channels. (C) 2017 Elsevier Ltd. All rights reserved.

Filiaciones:
Olamendi-Portugal, T.:
 Univ Nacl Autonoma Mexico, Dept Med Mol & Bioproc, Inst Biotecnol, Ave Univ 2001, Cuernavaca 62210, Morelos, Mexico

Csoti, A.:
 Univ Nacl Autonoma Mexico, Dept Fisiol, Fac Med, Mexico City 04510, DF, Mexico

Jimenez-Vargas, J. M.:
 Univ Nacl Autonoma Mexico, Dept Med Mol & Bioproc, Inst Biotecnol, Ave Univ 2001, Cuernavaca 62210, Morelos, Mexico

Gomez-Lagunas, F.:
 Univ Debrecen, Res Ctr Mol Med, Fac Med, Dept Biophys & Cell Biol, 1 Egyet Ter, H-4032 Debrecen, Hungary

Panyi, G.:
 Univ Nacl Autonoma Mexico, Dept Fisiol, Fac Med, Mexico City 04510, DF, Mexico

Possani, L. D.:
 Univ Nacl Autonoma Mexico, Dept Med Mol & Bioproc, Inst Biotecnol, Ave Univ 2001, Cuernavaca 62210, Morelos, Mexico
ISSN: 18793150
Editorial
PERGAMON-ELSEVIER SCIENCE LTD, THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND, Reino Unido
Tipo de documento: Article
Volumen: 133 Número:
Páginas: 136-144
WOS Id: 000403864000018
ID de PubMed: 28502745