“…Thus, perhaps in common with AKH structural features, the switch between adjacent hydrophobic and hydrophilic residues is necessary in order to properly ‘fit’ and bind with its particular receptor (Gäde and Hayes, 1995) so that not only is the ACP analog shorter by one amino acid (a nonapeptide), but moreover, the entire structural configuration of the peptide is disrupted and the whole sequence is no longer in sync with its receptor. This corroborates with studies that have examined the conservation of the ACP primary structures across insects from different orders (including Diptera, Lepidoptera, Coleoptera, Hymenoptera and Hemiptera) as well as from various species within the same order (seventeen species of Coleoptera), where the N-terminal pentamer sequence, when the ACP system is present, is nearly completely conserved across these various species with a consensus motif of pQVTFS-, whereas significant sequence variability occurs within the C-terminus of the ACP sequence with deca-, nona- and even dodecapeptides reported (Hansen et al, 2010; Veenstra, 2019).…”