Novel structural class of four disulfide-bridged peptides from Tityus serrulatus venom.
A new structural class of short peptides folded by four disulfide-bridges was found in the venom of the Brazilian scorpion Tityus serrulatus. Peptides were put on evidence independently by means of two different approaches of structurally guided prospection. First, a cDNA sequence was obtained using a degenerate primer constructed according to the C-terminal sequence of kaliotoxin (KTx2), from the Androctonus australis venom. Second, MALDI-TOF mass spectrometry analyses of toxic fraction FIII from T. serrulatus venom revealed a family of molecules ranging approximately from 2900 to 3000 Da. Three new peptides were isolated and named TsPep1, TsPep2, and TsPep3. Biochemical characterization showed that they are 29 amino acids long, constrained by a new pattern of four disulfide-bridges. These results enable us to classify these new molecules as part of a novel structural class of short peptides from scorpion venoms.
Pimenta
Adriano M C
AM
Laboratoire de Biochimie-Ingénierie des Protéines, UMR 6560-IFR Jean Roche, Université de la Méditerranée, Bd Pierre Dramard, 13916 20, Marseille Cedex, France. apimenta@icb.ufmg.br
Legros
Christian
C
Almeida
Flávia de Marco
Fde M
Mansuelle
Pascal
P
De Lima
Maria Elena
ME
Bougis
Pierre E
PE
Martin-Eauclaire
Marie France
MF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D004220:Disulfides / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D026902:Potassium Channel Blockers / Q000737:chemistry; D012604:Scorpion Venoms / Q000737:chemistry* / Q000235:genetics; D012605:Scorpions; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D018076:DNA, Complementary; D004220:Disulfides; D010455:Peptides; D026902:Potassium Channel Blockers; D012604:Scorpion Venoms