Kinetics of self-assembly of inclusions due to lipid membrane thickness interactions

10.1101/2020.09.23.309575 ◽

2020 ◽

Author(s):

Xinyu Liao ◽

Prashant K. Purohit

Keyword(s):

Self Assembly ◽

Time Scale ◽

Lipid Membranes ◽

Lipid Membrane ◽

First Passage Time ◽

Langevin Dynamics ◽

Passage Time ◽

Membrane Thickness ◽

Kinetics Of ◽

Two Inclusions

AbstractSelf-assembly of proteins on lipid membranes underlies many important processes in cell biology, such as, exo- and endo-cytosis, assembly of viruses, etc. An attractive force that can cause self-assembly is mediated by membrane thickness interactions between proteins. The free energy profile associated with this attractive force is a result of the overlap of thickness deformation fields around the proteins. The thickness deformation field around proteins of various shapes can be calculated from the solution of a boundary value problem and is relatively well understood. Yet, the time scales over which self-assembly occurs has not been explored. In this paper we compute this time scale as a function of the initial distance between two inclusions by viewing their coalescence as a first passage time problem. The first passage time is computed using both Langevin dynamics and a partial differential equation, and both methods are found to be in excellent agreement. Inclusions of three different shapes are studied and it is found that for two inclusions separated by about hundred nanometers the time to coalescence is hundreds of milliseconds irrespective of shape. Our Langevin dynamics simulation of self-assembly required an efficient computation of the interaction energy of inclusions which was accomplished using a finite difference technique. The interaction energy profiles obtained using this numerical technique were in excellent agreement with those from a previously proposed semi-analytical method based on Fourier-Bessel series. The computational strategies described in this paper could potentially lead to efficient methods to explore the kinetics of self-assembly of proteins on lipid membranes.Author summarySelf-assembly of proteins on lipid membranes occurs during exo- and endo-cytosis and also when viruses exit an infected cell. The forces mediating self-assembly of inclusions on membranes have therefore been of long standing interest. However, the kinetics of self-assembly has received much less attention. As a first step in discerning the kinetics, we examine the time to coalescence of two inclusions on a membrane as a function of the distance separating them. We use both Langevin dynamics simulations and a partial differential equation to compute this time scale. We predict that the time to coalescence is on the scale of hundreds of milliseconds for two inclusions separated by about hundred nanometers. The deformation moduli of the lipid membrane and the membrane tension can affect this time scale.

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Electrochemical Properties of Lipid Membranes Self-Assembled from Bicelles

Membranes ◽

10.3390/membranes11010011 ◽

2020 ◽

Vol 11 (1) ◽

pp. 11

Author(s):

Damian Dziubak ◽

Kamil Strzelak ◽

Slawomir Sek

Keyword(s):

Electrochemical Properties ◽

Self Assembly ◽

Lipid Membranes ◽

Lipid Membrane ◽

Membrane Resistance ◽

Electrochemical Characteristics ◽

Freeze Thaw ◽

Lipid Films ◽

Supported Lipid Membranes

Supported lipid membranes are widely used platforms which serve as simplified models of cell membranes. Among numerous methods used for preparation of planar lipid films, self-assembly of bicelles appears to be promising strategy. Therefore, in this paper we have examined the mechanism of formation and the electrochemical properties of lipid films deposited onto thioglucose-modified gold electrodes from bicellar mixtures. It was found that adsorption of the bicelles occurs by replacement of interfacial water and it leads to formation of a double bilayer structure on the electrode surface. The resulting lipid assembly contains numerous defects and pinholes which affect the permeability of the membrane for ions and water. Significant improvement in morphology and electrochemical characteristics is achieved upon freeze–thaw treatment of the deposited membrane. The lipid assembly is rearranged to single bilayer configuration with locally occurring patches of the second bilayer, and the number of pinholes is substantially decreased. Electrochemical characterization of the lipid membrane after freeze–thaw treatment demonstrated that its permeability for ions and water is significantly reduced, which was manifested by the relatively high value of the membrane resistance.

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Self-Healing Bilayer Lipid Membranes Formed Over Synthetic Substrates

Smart Materials, Adaptive Structures and Intelligent Systems, Volume 2 ◽

10.1115/smasis2008-460 ◽

2008 ◽

Author(s):

M. Austin Creasy ◽

Donald J. Leo

Keyword(s):

Self Assembly ◽

Lipid Membranes ◽

Lipid Membrane ◽

Bilayer Lipid Membrane ◽

Unique Property ◽

Bilayer Lipid Membranes ◽

Self Healing ◽

Electrical Field ◽

Bilayer Lipid ◽

Recent Experimental Study

Biological systems demonstrate autonomous healing of damage and are an inspiration for developing self-healing materials. Our recent experimental study has demonstrated that a bilayer lipid membrane (BLM), also called a black lipid membrane, has the ability to self-heal after mechanical failure. These molecules have a unique property that they spontaneously self assembly into organized structures in an aqueous medium. The BLM forms an impervious barrier to ions and fluid between two volumes and strength of the barrier is dependent on the pressure and electrical field applied to the membrane. A BLM formed over an aperture on a silicon substrate is shown to self-heal for 5 pressurization failure cycles.

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Self-assembly of monolayered lipid membranes for surface-coating of a nanoconfined Bombyx mori silk fibroin film

RSC Advances ◽

10.1039/c5ra09683a ◽

2015 ◽

Vol 5 (81) ◽

pp. 65684-65689 ◽

Cited By ~ 3

Author(s):

Fan Xu ◽

Meimei Bao ◽

Longfei Rui ◽

Jiaojiao Liu ◽

Jingliang Li ◽

...

Keyword(s):

Bombyx Mori ◽

Silk Fibroin ◽

Self Assembly ◽

Lipid Membranes ◽

Surface Coating ◽

Lipid Membrane ◽

Coating Film ◽

Silk Fibroin Film ◽

Bombyx Mori Silk ◽

Self Assembled

A self-assembled lipid membrane provides a smooth, hydrophilic and biocompatible surface coating film for materials.

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Assembling responsive microgels at responsive lipid membranes

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1807790116 ◽

2019 ◽

Vol 116 (12) ◽

pp. 5442-5450 ◽

Cited By ~ 11

Author(s):

Meina Wang ◽

Adriana M. Mihut ◽

Ellen Rieloff ◽

Aleksandra P. Dabkowska ◽

Linda K. Månsson ◽

...

Keyword(s):

Self Assembly ◽

Lipid Membranes ◽

Lipid Membrane ◽

Soft Materials ◽

Fluid Interfaces ◽

Biomedical Sciences ◽

Interfacial Assembly ◽

Colloidal Assembly ◽

Long Range Ordering ◽

Adsorption Desorption

Directed colloidal self-assembly at fluid interfaces can have a large impact in the fields of nanotechnology, materials, and biomedical sciences. The ability to control interfacial self-assembly relies on the fine interplay between bulk and surface interactions. Here, we investigate the interfacial assembly of thermoresponsive microgels and lipogels at the surface of giant unilamellar vesicles (GUVs) consisting of phospholipids bilayers with different compositions. By altering the properties of the lipid membrane and the microgel particles, it is possible to control the adsorption/desorption processes as well as the organization and dynamics of the colloids at the vesicle surface. No translocation of the microgels and lipogels through the membrane was observed for any of the membrane compositions and temperatures investigated. The lipid membranes with fluid chains provide highly dynamic interfaces that can host and mediate long-range ordering into 2D hexagonal crystals. This is in clear contrast to the conditions when the membranes are composed of lipids with solid chains, where there is no crystalline arrangement, and most of the particles desorb from the membrane. Likewise, we show that in segregated membranes, the soft microgel colloids form closely packed 2D crystals on the fluid bilayer domains, while hardly any particles adhere to the more solid bilayer domains. These findings thus present an approach for selective and controlled colloidal assembly at lipid membranes, opening routes toward the development of tunable soft materials.

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Reconstitution of ultrawide DNA origami pores in liposomes for transmembrane transport of macromolecules

10.1101/2021.02.24.432733 ◽

2021 ◽

Cited By ~ 1

Author(s):

Alessio Fragasso ◽

Nicola De Franceschi ◽

Pierre Stömmer ◽

Eli O. van der Sluis ◽

Hendrik Dietz ◽

...

Keyword(s):

Lipid Membranes ◽

Cell Biology ◽

Lipid Membrane ◽

Molecular Transport ◽

Dna Origami ◽

Influx Rate ◽

Membrane Pores ◽

Synthetic Cells ◽

Folded Proteins ◽

Membrane Spanning

AbstractMolecular traffic across lipid membranes is a vital process in cell biology that involves specialized biological pores with a great variety of pore diameters, from fractions of a nanometer to >30 nm. Creating artificial membrane pores covering similar size and complexity will aid the understanding of transmembrane molecular transport in cells, while artificial pores are also a necessary ingredient for synthetic cells. Here, we report the construction of DNA origami nanopores that have an inner diameter as large as 30 nm. We developed new methods to successfully insert these ultrawide pores into the lipid membrane of giant unilamellar vesicles (GUVs) by administering the pores concomitantly with vesicle formation in an inverted-emulsion cDICE technique. The reconstituted pores permit the transmembrane diffusion of large macromolecules such as folded proteins, which demonstrates the formation of large membrane-spanning open pores. The pores are size selective as dextran molecules with a diameter up to 22 nm can traverse the pores, whereas larger dextran molecules are blocked. By FRAP measurements and modelling of the GFP influx rate, we find that up to hundreds of pores can be functionally reconstituted into a single GUV. Our technique bears great potential for applications across different fields from biomimetics, synthetic biology, to drug delivery.

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In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

10.26434/chemrxiv.9876395.v1 ◽

2019 ◽

Author(s):

Hao Wu ◽

Jeffrey Ting ◽

Siqi Meng ◽

Matthew Tirrell

Keyword(s):

Small Angle ◽

Self Assembly ◽

Electrostatic Interactions ◽

Polyelectrolyte Complex ◽

Time Resolved ◽

X Ray ◽

X Ray Scattering ◽

Kinetics Of ◽

Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

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Interactions of Linear Analogues of Battacin with Negatively Charged Lipid Membranes

Membranes ◽

10.3390/membranes11030192 ◽

2021 ◽

Vol 11 (3) ◽

pp. 192

Author(s):

Kinga Burdach ◽

Dagmara Tymecka ◽

Aneta Urban ◽

Robert Lasek ◽

Dariusz Bartosik ◽

...

Keyword(s):

Lipid Membranes ◽

Liquid Crystalline ◽

Lipid Membrane ◽

Attenuated Total Reflection ◽

Gram Positive ◽

Insertion Depth ◽

Force Microscopy ◽

Acyl Chains ◽

Hydrophobic Portion ◽

Membrane Fluidization

The increasing resistance of bacteria to available antibiotics has stimulated the search for new antimicrobial compounds with less specific mechanisms of action. These include the ability to disrupt the structure of the cell membrane, which in turn leads to its damage. In this context, amphiphilic lipopeptides belong to the class of the compounds which may fulfill this requirement. In this paper, we describe two linear analogues of battacin with modified acyl chains to tune the balance between the hydrophilic and hydrophobic portion of lipopeptides. We demonstrate that both compounds display antimicrobial activity with the lowest values of minimum inhibitory concentrations found for Gram-positive pathogens. Therefore, their mechanism of action was evaluated on a molecular level using model lipid films mimicking the membrane of Gram-positive bacteria. The surface pressure measurements revealed that both lipopeptides show ability to bind and incorporate into the lipid monolayers, resulting in decreased ordering of lipids and membrane fluidization. Atomic force microscopy (AFM) imaging demonstrated that the exposure of the model bilayers to lipopeptides leads to a transition from the ordered gel phase to disordered liquid crystalline phase. This observation was confirmed by attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR) results, which revealed that lipopeptide action causes a substantial increase in the average tilt angle of lipid acyl chains with respect to the surface normal to compensate for lipopeptide insertion into the membrane. Moreover, the peptide moieties in both molecules do not adopt any well-defined secondary structure upon binding with the lipid membrane. It was also observed that a small difference in the structure of a lipophilic chain, altering the balance between hydrophobic and hydrophilic portion of the molecules, results in different insertion depth of the active compounds.

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Controlling the Kinetics of an Enzymatic Reaction through Enzyme or Substrate Confinement into Lipid Mesophases with Tunable Structural Parameters

International Journal of Molecular Sciences ◽

10.3390/ijms21145116 ◽

2020 ◽

Vol 21 (14) ◽

pp. 5116

Author(s):

Marco Mendozza ◽

Arianna Balestri ◽

Costanza Montis ◽

Debora Berti

Keyword(s):

Reaction Kinetics ◽

Self Assembly ◽

Liquid Crystalline ◽

Structural Parameters ◽

Enzymatic Reaction ◽

X Ray Scattering ◽

Nitrophenyl Phosphate ◽

Vis Spectroscopy ◽

Kinetics Of ◽

Enzyme Alkaline Phosphatase

Lipid liquid crystalline mesophases, resulting from the self-assembly of polymorphic lipids in water, have been widely explored as biocompatible drug delivery systems. In this respect, non-lamellar structures are particularly attractive: they are characterized by complex 3D architectures, with the coexistence of hydrophobic and hydrophilic regions that can conveniently host drugs of different polarities. The fine tunability of the structural parameters is nontrivial, but of paramount relevance, in order to control the diffusive properties of encapsulated active principles and, ultimately, their pharmacokinetics and release. In this work, we investigate the reaction kinetics of p-nitrophenyl phosphate conversion into p-nitrophenol, catalysed by the enzyme Alkaline Phosphatase, upon alternative confinement of the substrate and of the enzyme into liquid crystalline mesophases of phytantriol/H2O containing variable amounts of an additive, sucrose stearate, able to swell the mesophase. A structural investigation through Small-Angle X-ray Scattering, revealed the possibility to finely control the structure/size of the mesophases with the amount of the included additive. A UV–vis spectroscopy study highlighted that the enzymatic reaction kinetics could be controlled by tuning the structural parameters of the mesophase, opening new perspectives for the exploitation of non-lamellar mesophases for confinement and controlled release of therapeutics.

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