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Scorpine, an anti‐malaria and anti‐bacterial agent purified from scorpion venom
Author(s) -
Conde Renaud,
Zamudio Fernando Z.,
Rodrı́guez Mario H.,
Possani Lourival D.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01384-3
Subject(s) - venom , scorpion , plasmodium berghei , peptide , peptide sequence , complementary dna , amino acid , cdna library , biology , microbiology and biotechnology , molecular mass , biochemistry , chemistry , gene , malaria , immunology , enzyme
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 μM) and gamete (ED 50 10 μM) 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.