Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta

Analysis of the structural and binding properties of the C-terminus, 4K peptide of apolipophorin III (apoLp-III), an apolipoprotein from Manduca sexta, helps study the interaction between apoLp-III lipoprotein membrane and phospholipids. The 4K peptide lacks the ability to bind to lipoprotein surfaces and to convert phospholipid bilayers to discs, indicating that other regions in the molecule contribute to the interaction with lipoproteins and phospholipid bilayers. However, the 4K peptide is capable of forming an amphipathic helix.