Immunogenicity of a synthetic HBsAg peptide: enhancement by conjugation to a fatty acid carrier.
Effective immunization with short polypeptide antigens has typically only been possible when the peptide is conjugated to a large carrier substance, usually a protein. Such immunizations suffer from difficulties in producing conjugates of reliable composition, and from unwanted anti-carrier immune responses. When a chemically synthesized peptide, bearing hepatitis B virus a-determinant specificity, was conjugated to a dipalmityl-lysine moiety, a significant improvement in anti-hepatitis B surface antigen response was obtained, in comparison to the corresponding peptide-keyhole limpet hemocyanin conjugate. Dipalmityl lysyl peptide conjugates are readily made by standard Merrifield synthesis procedures, and are relatively free of byproducts that might cause unwanted immune responses. Gel filtration experiments suggest that the conjugates form large aggregates, possibly micelles, which may play a significant role in the enhancement of the anti-peptide response. These properties suggest that fatty acid conjugation may be a useful procedure for producing chemically synthesized peptide vaccines.
D000818:Animals; D006510:Hepatitis B Antibodies / Q000096:biosynthesis*; D006514:Hepatitis B Surface Antigens / Q000276:immunology*; D008239:Lysine / Q000031:analogs & derivatives* / Q000276:immunology; D010169:Palmitic Acids / Q000276:immunology*; D010455:Peptides / Q000276:immunology*; D011817:Rabbits
D006510:Hepatitis B Antibodies; D006514:Hepatitis B Surface Antigens; D010169:Palmitic Acids; D010455:Peptides; C040806:N(2),N(6)-dipalmitoyllysine; D008239:Lysine