scholarly journals Exploring the structural relationship between encapsulated antimicrobial peptides and the bilayer membrane mimetic lipidic cubic phase: studies with gramicidin A′

RSC Advances ◽  
2016 ◽  
Vol 6 (73) ◽  
pp. 68685-68694 ◽  
Author(s):  
Thomas G. Meikle ◽  
Charlotte E. Conn ◽  
Frances Separovic ◽  
Calum J. Drummond
Keyword(s):  
Antimicrobial Peptides ◽  
Low Cost ◽  
Bilayer Membrane ◽  
Structural Relationship ◽  
Gramicidin A ◽  
Cubic Phase ◽  
Membrane Peptides ◽  
Membrane Mimetic ◽  
Lipidic Cubic Phase ◽  
Bicontinuous Cubic

Lipid based bicontinuous cubic mesophases provide a low-cost, robust membrane mimetic nanomaterial which allows for the incorporation of membrane peptides and proteins.

scholarly journals The Lipidic Cubic Phase as a Membrane Mimetic

2011 ◽  
Vol 100 (8) ◽  
pp. 2075 ◽  
Author(s):  
Nicole Höfer ◽  
David Aragão ◽  
Martin Caffrey
Keyword(s):  
Cubic Phase ◽  
Membrane Mimetic ◽  
Lipidic Cubic Phase

scholarly journals Renaturing Membrane Proteins in the Lipid Cubic Phase, a Nanoporous Membrane Mimetic

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Dianfan Li ◽  
Martin Caffrey
Keyword(s):  
Membrane Proteins ◽  
Diacylglycerol Kinase ◽  
Phase Method ◽  
Cubic Phase ◽  
X Ray ◽  
Nanoporous Membrane ◽  
Membrane Mimetic ◽  
Test Protein ◽  
Bicontinuous Cubic

Abstract Membrane proteins play vital roles in the life of the cell and are important therapeutic targets. Producing them in large quantities, pure and fully functional is a major challenge. Many promising projects end when intractable aggregates or precipitates form. Here we show how such unfolded aggregates can be solubilized and the solution mixed with lipid to spontaneously self-assemble a bicontinuous cubic mesophase into the bilayer of which the protein, in a confined, chaperonin-like environment, reconstitutes with 100% efficiency. The test protein, diacylglycerol kinase, reconstituted in the bilayer of the mesophase, was then crystallized in situ by the in meso or lipid cubic phase method providing an X-ray structure to a resolution of 2.55 Å. This highly efficient, inexpensive, simple and rapid approach should find application wherever properly folded, membrane reconstituted and functional proteins are required where the starting material is a denatured aggregate.

Low-pH-Induced Transformation of Bilayer Membrane into Bicontinuous Cubic Phase in Dioleoylphosphatidylserine/Monoolein Membranes

Langmuir ◽  
2008 ◽  
Vol 24 (7) ◽  
pp. 3400-3406 ◽  
Author(s):  
Yoshihide Okamoto ◽  
Shah Md. Masum ◽  
Haruna Miyazawa ◽  
Masahito Yamazaki
Keyword(s):  
Bilayer Membrane ◽  
Low Ph ◽  
Cubic Phase ◽  
Bicontinuous Cubic

scholarly journals Serial femtosecond crystallography of soluble proteins in lipidic cubic phase

IUCrJ ◽  
2015 ◽  
Vol 2 (5) ◽  
pp. 545-551 ◽  
Author(s):  
Raimund Fromme ◽  
Andrii Ishchenko ◽  
Markus Metz ◽  
Shatabdi Roy Chowdhury ◽  
Shibom Basu ◽  
...  
Keyword(s):  
Data Collection ◽  
Protein Structure Determination ◽  
Soluble Proteins ◽  
Cubic Phase ◽  
Data Sets ◽  
Carrier Medium ◽  
X Ray ◽  
Membrane Mimetic ◽  
Lipidic Cubic Phase ◽  
Serial Femtosecond Crystallography

Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) enables high-resolution protein structure determination using micrometre-sized crystals at room temperature with minimal effects from radiation damage. SFX requires a steady supply of microcrystals intersecting the XFEL beam at random orientations. An LCP–SFX method has recently been introduced in which microcrystals of membrane proteins are grown and delivered for SFX data collection inside a gel-like membrane-mimetic matrix, known as lipidic cubic phase (LCP), using a special LCP microextrusion injector. Here, it is demonstrated that LCP can also be used as a suitable carrier medium for microcrystals of soluble proteins, enabling a dramatic reduction in the amount of crystallized protein required for data collection compared with crystals delivered by liquid injectors. High-quality LCP–SFX data sets were collected for two soluble proteins, lysozyme and phycocyanin, using less than 0.1 mg of each protein.

Triply-periodic nanostructures in surfactant, block copolymer, and biomembrane systems, and simulation of TEMs

1993 ◽  
Vol 51 ◽  
pp. 884-885
Author(s):  
David M. Anderson ◽  
Tomas Landh
Keyword(s):  
Liquid Crystalline ◽  
Diblock Copolymers ◽  
Cubic Phase ◽  
List Type ◽  
Interpenetrating Networks ◽  
Triply Periodic ◽  
Wide Range ◽  
Bicontinuous Cubic ◽  
Phase Liquid ◽  
Dividing Surface

First discovered in surfactant-water liquid crystalline systems, so-called ‘bicontinuous cubic phases’ have the property that hydropnilic and lipophilic microdomains form interpenetrating networks conforming to cubic lattices on the scale of nanometers. Later these same structures were found in star diblock copolymers, where the simultaneous continuity of elastomeric and glassy domains gives rise to unique physical properties. Today it is well-established that the symmetry and topology of such a morphology are accurately described by one of several triply-periodic minimal surfaces, and that the interface between hydrophilic and hydrophobic, or immiscible polymer, domains is described by a triply-periodic surface of constant, nonzero mean curvature. One example of such a dividing surface is shown in figure 5.The study of these structures has become of increasing importance in the past five years for two reasons:1)Bicontinuous cubic phase liquid crystals are now being polymerized to create microporous materials with monodispersed pores and readily functionalizable porewalls; figure 3 shows a TEM from a polymerized surfactant / methylmethacrylate / water cubic phase; and2)Compelling evidence has been found that these same morphologies describe biomembrane systems in a wide range of cells.

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