A generic method is reported for the assembly of multi-peptide polymers in which peptides are synthesized in the solid phase, the N-terminal residue acryloylated, and the derivitized peptides cleaved, purified and finally polymerized by free radical induced polymerization. The high molecular weight polymers generated in this way have individual peptides pendant from a backbone support. Incorporation of 6-aminohexanoyl or other residue(s) at the N-terminus of the peptide prior to acryloylation allows the peptide to be distanced from the polymer backbone and incorporation of acryloylated reagents into the polymerization mixture also permits distancing of pendant peptides along the length of the backbone support. The polymerization process results in highly antigenic artificial proteins as measured by ELISA. Because this approach allows the incorporation of the same or combinations of different purified peptides into polymers, it lends itself to the assembly of potential vaccine candidates containing epitopes from single or multiple pathogens into a single covalent structure.