Influence of poly(L-lysine) on the structure of dipalmitoylphosphatidylglycerol/water dispersions studied by X-ray scattering

• Published in: European biophysics journal Vol. 36; no. 4-5; pp. 425 - 435
• Main Authors: Förster, G, Schwieger, C, Faber, F, Weber, T, Blume, A
• Format: Journal Article
• Language: English
• Published: Germany Springer Nature B.V 01.04.2007
• Subjects: Colloids - chemistry; Computer Simulation; Conformation; Crystal structure; Crystallinity; Crystallization; Dispersions; Freezing; Freezing point; Helices; Lipid Bilayers - chemistry; Lipids; Liposomes - chemistry; Low temperature; Lysine; Melting points; Models, Chemical; Models, Molecular; Molecular Conformation; Phase transitions; Phosphatidylglycerols - chemistry; Phospholipids; Polylysine - chemistry; Protein structure; Recrystallization; Salts; Secondary structure; Small angle X ray scattering; Solutions; Structural models; Water - chemistry; X-Ray Diffraction - methods; X-ray scattering
• ISSN: 0175-7571; 1432-1017
• DOI: 10.1007/s00249-006-0087-1

The interaction between the negatively charged phospholipid DPPG and positively charged poly(L: -lysine) (PLL) of different lengths was studied by X-ray scattering in the SAXS and WAXS region. As a reference pure DPPG (Na salt) was investigated over a wide temperature range (-30 to 70 degrees C). The phase behavior of DPPG in aqueous and in buffer/salt dispersions showed a metastable subgel phase at low temperatures and a recrystallization upon heating before reaching the liquid-crystalline phase. The presence of additional salt stabilizes the bilayer structure and decreases the recrystallization temperature. Large changes in the SAXS region are not connected with changes in chain packing. In DPPG/PLL samples, the PLL is inserted between adjacent headgroup layers and liberates counterions which give rise to a freezing point depression. In the complex with DPPG PLL form an alpha-helical secondary structure at pH 7 and temperatures below the gel to liquid-crystalline phase transition. This prevents DPPG from recrystallization and strongly increases the stacking order. The lamellar repeat distance is decreased and fixed by the helix conformation of PLL in the gel phase. PLL with n = 14 is too short to form helices and is squeezed out reversibly from the interbilayer space upon cooling by freezing of trapped water. In dispersions with longer PLLs (n > 400) at -20 degrees C a 1D crystallization of PLL alpha-helices in the aqueous layer between the headgroups takes place. A structural model is presented for the lateral periodic complex, which is similar to the known cationic lipid/DNA complex.