Far-u.v. CD-spectroscopy and immunological properties of synthetic sequential peptides derived from cardiotoxin VII1 of Naja nivea venom: an amphipathic alpha-helix formed by sequence 15-25 of a beta-protein.
1. Immunological properties of cardiotoxin V(II)1 of Naja nivea were investigated. 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. The conformation of each synthetic peptide in various solvents was determined by circular dichroism spectroscopy for relating immunological to structural properties. 4. It was found that sequential epitopes are absent in this cardiotoxin, but that region 15-25, although part of a beta-structured region, could be a possible T-cell epitope through the formation of an amphipathic helix.
Osthoff
G
G
Division of Processing and Chemical Manufacturing Technology, CSIR, Pretoria, Republic of South Africa.
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D004179:Cobra Cardiotoxin Proteins / Q000276:immunology*; D004546:Elapid Venoms / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D006168:Guinea Pigs; D005779:Immunodiffusion; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology*; D011487:Protein Conformation
D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms; D000939:Epitopes; D010446:Peptide Fragments