A conformationally constrained synthetic peptide efficiently inhibits malaria parasite entry into human red blood cells

Abstract

Restricting the conformational freedom of a peptide by backbone cyclization and incorporation of an additional disulfide bond leads to a unique cyclic peptide that inhibits the invasion of red blood cells by malaria parasites efficiently. The engineered peptide exhibits twenty fold enhanced affinity towards its receptor (PfAMA1) compared to the native peptide ligand (PfRON2).