A self-associating hepatitis B surface antigen-derived peptide that is immunogenic in alum

We previously described an oligomeric synthetic peptide derived from the hepatitis B surface antigen that displayed a limited tendency to form self-associating macromolecular structures in solution. Here it is demonstrated that amino-terminal myristylation of this peptide results in near quantitative aggregation of the oligomeric peptide. The myristylated peptide is highly immunogenic when used in conjunction with alum as adjuvant in both the rabbit and rhesus monkey models. The antibody response generated by peptide also cross-reacted with native antigen and was long-lasting. Collectively the results described in this and previous reports offer an attractive new approach for generating immunogenic peptide mimetics of conformational epitopes that may find application as vaccines.