Phase diagrams of systems with cationic α-helical membrane-spanning model peptides and dioleoylphosphatidylcholine
2001 (English)In: Advances in Colloid and Interface Science, Vol. 89-90, no 239-61Article in journal (Refereed) Published
Ternary phase diagrams have been constructed of systems with dioleoylphosphatidylcholine (DOPC) and water, and two α-helical membrane-spanning model peptides, KKLAKK16[KK(LA)6KK] and KKLAKK20[KK(LA)8KK]. It was found that these peptides induced non-lamellar liquid crystalline phases. The amount of peptide needed for this phase transition depended on the water content and the temperature; and for KKLAKK16, a smaller amount of peptide was needed to induce non-lamellar phases than for KKLAKK20. Both peptides were found to induce an isotropic phase, and KKLAKK16 also induced a reversed hexagonal phase. Both peptides may also reside in a lamellar (Lα) phase. When magic angle spinning (MAS) 31P NMR experiments were performed on samples containing the Lα phase and an isotropic phase, four different isotropic chemical shifts were observed. The isotropic chemical shifts could be assigned to the phases, using spinning sidebands to calculate the chemical shift anisotropy (CSA) corresponding to each isotropic shift. MAS 13C NMR also indicated a difference in the aggregational state of the peptides between the Lα and isotropic phases. The phase diagrams were compared to the phase diagram of a similar model peptide, AWW(LA)5WWA in systems with DOPC and water. It was concluded that the phase behaviour was influenced by both electrostatic interactions between the peptides and the lipid headgroups, and the difference between the hydrophobic length of the peptide and the hydrophobic thickness of the lipid bilayer.
Place, publisher, year, edition, pages
2001. Vol. 89-90, no 239-61
31P NMR, 13C NMR, 2H NMR, MAS NMR, Lamellar phases, Hexagonal phases, Hydrophobic mismatch
IdentifiersURN: urn:nbn:se:umu:diva-8631DOI: doi:10.1016/S0001-8686(00)00056-7OAI: oai:DiVA.org:umu-8631DiVA: diva2:148302