Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures  

作　　者：Karin Kornmueller  Bernhard Lehofer  Gerd Leitinger  Heinz Amenitsch  Ruth Prassl 

机构地区：[1]Institute of Biophysics Medical University of Graz, BioTechMed-Graz Graz Austria [2]Institute of Cell Biology, Histology and Embryology, Research Unit Electron Microscopic Techniques Medical University of Graz Graz Austria [3]Institute of Inorganic Chemistry Graz University of Technology Graz Austria

出　　处：《Nano Research》2018年第2期913-928,共16页纳米研究（英文版）

摘　　要：Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as the most relevant biological representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates （V4D, V4WD, V4WD2, I4WD2） readily self-assembled into lamellae in aqueous solution. Small-angle X-ray scattering （SAXS） patterns revealed ordered lamellar structures with a repeat distance of 4-5 nm. Transmission electron microscopy （TEM） images confirmed the presence of stacked sheets. Two derivatives （V3D and V4D2） remained as loose aggregates dispersed in solution; one peptide （L4WD2） formed twisted tapes with internal lameUae and an antiparaUel -type monomer aligrtment. To understand the interaction of peptides with lipids, they were mixed with phosphatidylcholines. Low peptide concentrations （1.1 mM） induced the formation of a heterogeneous mixture of vesicular structures. Large multilamellar vesicles （MLV, d-spacing - 6.3 nm） coexisted with oligo- or unilamellar vesicles （- 50 nm in diameter） and bicelle-like structures （- 45 nm length, - 18 nm width）. High peptide concentrations （11 mM） led to unilamellar vesicles （ULV, diameter - 260-280 nm） with a homogeneous mixing of lipids and peptides. SAXS revealed the temperature-dependent fine structure of these ULVs. At 25 ℃ the bilayer is in a fully Interdigitated state （headgroup-to-headgroup distance dH, -2.9 nm）, whereas at 50 ℃this interdigitation opens up （dtm- 3.6 nm）. Our results highlight the versatility of self-assembled peptide superstructures. Subtle changes in the amino acid composition are key design elements in creating peptide- or lipid- peptide nanostructures with richness in morphology similar to that of naturally occurrin~ lioids.Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as the most relevant biological representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates （V4D, V4WD, V4WD2, I4WD2） readily self-assembled into lamellae in aqueous solution. Small-angle X-ray scattering （SAXS） patterns revealed ordered lamellar structures with a repeat distance of 4-5 nm. Transmission electron microscopy （TEM） images confirmed the presence of stacked sheets. Two derivatives （V3D and V4D2） remained as loose aggregates dispersed in solution; one peptide （L4WD2） formed twisted tapes with internal lameUae and an antiparaUel -type monomer aligrtment. To understand the interaction of peptides with lipids, they were mixed with phosphatidylcholines. Low peptide concentrations （1.1 mM） induced the formation of a heterogeneous mixture of vesicular structures. Large multilamellar vesicles （MLV, d-spacing - 6.3 nm） coexisted with oligo- or unilamellar vesicles （- 50 nm in diameter） and bicelle-like structures （- 45 nm length, - 18 nm width）. High peptide concentrations （11 mM） led to unilamellar vesicles （ULV, diameter - 260-280 nm） with a homogeneous mixing of lipids and peptides. SAXS revealed the temperature-dependent fine structure of these ULVs. At 25 ℃ the bilayer is in a fully Interdigitated state （headgroup-to-headgroup distance dH, -2.9 nm）, whereas at 50 ℃this interdigitation opens up （dtm- 3.6 nm）. Our results highlight the versatility of self-assembled peptide superstructures. Subtle changes in the amino acid composition are key design elements in creating peptide- or lipid- peptide nanostructures with richness in morphology similar to that of naturally occurrin~ lioids.

关 键 词：amphiphilic designerpeptides lipids NANOSTRUCTURES LAMELLAE small-angle X-rayscattering （SAXS） transmission electronmicroscopy （TEM） 

分 类 号：O734.1[理学—晶体学] TQ658[化学工程—精细化工]