Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Protein science : a publication of the Protein Society. Année : 2006

Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum

Résumé

Psalmopeotoxin I (PcFK1) is a 33-amino-acid residue peptide isolated from the venom of the tarantula Psalmopoeus cambridgei. It has been recently shown to possess strong antiplasmodial activity against the intra-erythrocyte stage of Plasmodium falciparum in vitro. Although the molecular target for PcFK1 is not yet determined, this peptide does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. We investigated the structural properties of PcFK1 to help understand the unique mechanism of action of this peptide and to enhance its utility as a lead compound for rational development of new antimalarial drugs. In this paper, we have determined the three-dimensional solution structure by 1H two-dimensional NMR means of recombinant PcFK1, which is shown to belong to the ICK structural superfamily with structural determinants common to several neurotoxins acting as ion channels effectors.
Fichier sous embargo
Fichier sous embargo
Date de visibilité indéterminée
Loading...

Dates et versions

hal-00018558 , version 1 (06-02-2006)

Identifiants

Citer

Cyril Pimentel, Soo-Jin Choi, Benjamin Chagot, Catherine Guette, Jean-Michel Camadro, et al.. Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum. Protein science : a publication of the Protein Society., 2006, 15(3), pp.628-34. ⟨10.1110/ps.051860606⟩. ⟨hal-00018558⟩
116 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More