It could be concluded that the disordered repeats and/or the relative position variations of N-and C-terminal α-helices, interfered with 24C dockingaffinities. The CSP disordered repeats may have unknown functions with stretches without any folding (intrinsically disordered) or with conditional folding . Intrinsically disordered domains may be highly dynamic changing their conformations to favour antibody escape to protect the C-terminal CSP functions . Docking recognition of intrinsically disordered repeats may be challenging, as shown for some viral nucleoproteins (i.e, 51 % intrinsically disordered nucleocapsid of SARS-CoV-2) . On the other hand, some of the CSP disordered repeats may be conditional, getting some fold after additional protein interactions such as those spiral repeat conformations induced by mAb850 binding . Alphafold cannot yet predict such flexibilities since their predicted models are only accurate at the crystalized αTSR domains . In contrast to intrinsically disordered or conditional folding repeats (difficult to target by docking because possible multiple, transient and/or non-specific interactions), the well known CSP folded motifs may be more reliable to target for docking (i.e., hydrophobic cavities described by crystallographic analysis 27 ). Did SP removal altered CSP docking? One of the concerns about targeting CSP 24C was due to the temporary presence of the SP. SPs are ~ 20 mer α-helices located at the Nterminal nascent chains of the proteins to be secreted. Since SPs are cotranslationally removed after the proteins are translocated to the membranes of the endoplasmic reticulum, the SP α-helix of 24C should be absent on the surface of migratory circumsporozoites . Therefore, the 24C only could be targeted shortly during CSP intracellular biosynthesis, whether inside the hepatocyte and/or at the erythrocytes. Examples of co-translational translocation inhibitors targeting SPs specifically are beginning to appear as possible new drug targets , therefore, it may be possible that some top-children conformers targeting 24C could inhibit CSP during its biosynthesis.