Localization of the toxic site of naja mossambica cardiotoxins: Small synthetic peptides express an in vivo lethality

• Published in: Biochemical and biophysical research communications Vol. 153; no. 2; pp. 642 - 647
• Main Authors: Marchot, P., Bougis, P.E., Ceard, B., Van Rietschoten, J., Rochat, H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 16.06.1988; Elsevier
• Subjects: Amino Acid Sequence; Animal biology; Animals; Cobra Cardiotoxin Proteins - toxicity; Elapid Venoms - toxicity; Lethal Dose 50; Life Sciences; Male; Mice; Molecular Sequence Data; Peptide Fragments - toxicity; Peptides - chemical synthesis; Peptides - toxicity; Spectrophotometry, Ultraviolet; Structure-Activity Relationship
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(88)81143-4

Cardiotoxins are small basic proteins which cause heart failure when they are injected in viva In order to better understand their molecular mode of action, short peptides designed on the model of the first loop of the molecule of cardiotoxin IV from Naja mossambica mossambica venom have been synthetized by the solid-phase procedure of Merrifield. These peptides express lethality in mouse when they are injected intravenously. Taking into account the respective molecular weights, they are 3.5 to 5% as toxic as the cardiotoxin. Furthermore, the symptomatology they induce is undistinguishable from that induced by cardiotoxins. These results strongly support our previous hypothesis that the first loop of the molecule is the toxic site of cardiotoxins.