We addressed this challenge by combining bioinformatics, chemical peptide synthesis and functional protection assays. We focused on the search for a-helical coiled coil motifs that, in general, do not exhibit a folding problem, and are a target of effective antibodies for several current malaria vaccine candidates (eg. LSA-1 [3] , LSA-3 [4] , MSP-3 [5] , and MSP-6 [6] and other pathogens [7] . MSP-1, another leading malaria vaccine [8] , also contains predicted a-helical coiled coil regions (unpublished results). Our choice was based on the following considerations. First, the a-helical coiled coil motif bears a characteristic seven amino acid residue repeat (abcdefg) n with hydrophobic residues located in a and d positions and hydrophilic residues generally elsewhere. This motif can be easily identified by bioinformatic analysis. Secondly, an important known characteristic of the ahelical coiled coil domains is that, taken separately from the whole protein, they frequently and readily fold into the same stable oligomeric structure [9] . Thirdly, for this reason, the a-helical coiled coil fragments are frequently recognized by conformational dependent antibodies, and can similarly elicit antibodies reactive with structurally ''native'' epitopes. In addition, these domains are short (about 40 residues) and can be rapidly produced by chemical synthesis. Furthermore, when the antibodies have an anti-parasite biological activity, this designates the corresponding proteins/ fragments as potential, novel vaccine candidates to be further developed and assessed. Here, we focus on the Pf parasite erythrocytic stage, a target of protective antibodies and describe a straightforward, rapid procedure based on bioinformatic analysis of a-helical coiled-coil motifs and peptide synthesis.