FEBS Letters · 2000 · 280 citations · 10 references
MedicinePharmacologyBiochemical PharmacologyDrug DiscoveryMolecular PharmacologyAntimicrobial PeptidesAntiparasitic AgentsAntiparasitic PharmacologyEnzyme InhibitionPeptide ChemistryVenom BiologyAmino AcidsAntibacterial PeptidesCdna CloningCdna Library ConstructionDisulfide ChemistryMolecular Mass DeterminationSnake Venom CompositionVenom Pharmacology
A novel peptide, scorpine, was isolated from the venom of the scorpion Pandinus imperator, with anti-bacterial activity and a potent inhibitory effect on the ookinete (ED(50) 0.7 microM) and gamete (ED(50) 10 microM) stages of Plasmodium berghei development. It has 75 amino acids, three disulfide bridges with a molecular mass of 8350 Da. Scorpine has a unique amino acid sequence, similar only to some cecropins in its N-terminal segment and to some defensins in its C-terminal region. Its gene was cloned from a cDNA library.
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Stéphane Cociancich, M. Goyffon, François Bontems et al. · Biochemical and Biophysical Research Communications · 1993 · 172 citations
Philippe Bulet, Stéphane Cociancich, Michel REULAND et al. · European Journal of Biochemistry · 1992 · 120 citations · Full text