Far-u.v. cd-spectroscopy and immunological properties of synthetic sequential peptides derived from cardiotoxin v II1 of Naja nivea venom: An amphipathic α-helix formed by sequence 15–25 of a β-protein

Abstract

1. 1. Immunological properties of cardiotoxin V II1 of Naja nivea were investigated. 2. 2. Polyvalent antiserum raised against the cardiotoxin was tested for its interaction with synthetic peptides of overlapping sequence in order to locate possible sequential epitopes. 3. 3. The conformation of each synthetic peptide in various solvents was determined by circular dichroism spectroscopy for relating immunological to structural properties. 4. 4. It was found that sequential epitopes are absent in this cardiotoxin, but that region 15–25, although part of a β-structured region, could be a possible T-eell epitope through the formation of an amphipathic helix.