Plasmodium vivax CS peptides display conformational preferences for folded forms in solution.

Spectroscopic techniques have been used to study the conformations of several synthetic peptides with sequences corresponding to the repeat regions of the circumsporozoite proteins of Plasmodium vivax, variants vk-210 and vk-247. As has previously been shown for P. falciparum, turn-like folded conformations are observed, in rapid dynamic equilibrium with extended-chain forms. These results are consistent with the known similarity of the structural, biosynthetic and immunological properties of the circumsporozoite proteins of different plasmodial species. Additionally, the observation of folded conformers provides a rationale for the effectiveness of these peptides as immunogens and potential vaccines.