Ionic Hydrogen Bonds and Lipid Packing Defects Determine the Binding Orientation and Insertion Depth of RecA on Multicomponent Lipid Bilayers

2016 ◽  
Vol 120 (33) ◽  
pp. 8424-8437 ◽  
Author(s):  
Leili Zhang ◽  
Manohary Rajendram ◽  
Douglas B. Weibel ◽  
Arun Yethiraj ◽  
Qiang Cui
Keyword(s):  
Hydrogen Bonds ◽  
Lipid Bilayers ◽  
Insertion Depth ◽  
Lipid Packing ◽  
Packing Defects ◽  
Binding Orientation ◽  
Ionic Hydrogen Bonds

scholarly journals α-Synuclein Senses Lipid Packing Defects and Induces Lateral Expansion of Lipids Leading to Membrane Remodeling

2013 ◽  
Vol 288 (29) ◽  
pp. 20883-20895 ◽  
Author(s):  
Myriam M. Ouberai ◽  
Juan Wang ◽  
Marcus J. Swann ◽  
Celine Galvagnion ◽  
Tim Guilliams ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Lipid Membranes ◽  
Binding Mode ◽  
Lateral Expansion ◽  
Optical Biosensing ◽  
Lipid Packing ◽  
Force Microscopy ◽  
Packing Defects ◽  
Lipid Environment ◽  
Dynamic Structures

There is increasing evidence for the involvement of lipid membranes in both the functional and pathological properties of α-synuclein (α-Syn). Despite many investigations to characterize the binding of α-Syn to membranes, there is still a lack of understanding of the binding mode linking the properties of lipid membranes to α-Syn insertion into these dynamic structures. Using a combination of an optical biosensing technique and in situ atomic force microscopy, we show that the binding strength of α-Syn is related to the specificity of the lipid environment (the lipid chemistry and steric properties within a bilayer structure) and to the ability of the membranes to accommodate and remodel upon the interaction of α-Syn with lipid membranes. We show that this interaction results in the insertion of α-Syn into the region of the headgroups, inducing a lateral expansion of lipid molecules that can progress to further bilayer remodeling, such as membrane thinning and expansion of lipids out of the membrane plane. We provide new insights into the affinity of α-Syn for lipid packing defects found in vesicles of high curvature and in planar membranes with cone-shaped lipids and suggest a comprehensive model of the interaction between α-Syn and lipid bilayers. The ability of α-Syn to sense lipid packing defects and to remodel membrane structure supports its proposed role in vesicle trafficking.

Hydroxyl Ionic Liquids: The Differentiating Effect of Hydroxyl on Polarity due to Ionic Hydrogen Bonds between Hydroxyl and Anions

2010 ◽  
Vol 114 (11) ◽  
pp. 3912-3920 ◽  
Author(s):  
Shiguo Zhang ◽  
Xiujuan Qi ◽  
Xiangyuan Ma ◽  
Liujin Lu ◽  
Youquan Deng
Keyword(s):  
Ionic Liquids ◽  
Hydrogen Bonds ◽  
Ionic Hydrogen Bonds

scholarly journals Lipid packing defects and membrane charge control RAB GTPase recruitment

Traffic ◽  
2018 ◽  
Vol 19 (7) ◽  
pp. 536-545 ◽  
Author(s):  
Guillaume Kulakowski ◽  
Hugo Bousquet ◽  
Jean-Baptiste Manneville ◽  
Patricia Bassereau ◽  
Bruno Goud ◽  
...  
Keyword(s):  
Rab Gtpase ◽  
Lipid Packing ◽  
Charge Control ◽  
Membrane Charge ◽  
Packing Defects

THERMOREVERSIBLE CROSS-LINKING MALEIC ANHYDRIDE GRAFTED CHLOROBUTYL RUBBER WITH HYDROGEN BONDS (COMBINED WITH IONIC INTERACTIONS)

2014 ◽  
Vol 87 (3) ◽  
pp. 459-470 ◽  
Author(s):  
Lin Li ◽  
Jin Kuk Kim
Keyword(s):  
Hydrogen Bonds ◽  
Maleic Anhydride ◽  
Ionic Interactions ◽  
Cross Linking ◽  
External Energy ◽  
Scanning Calorimetry ◽  
Ionic Bonds ◽  
Cross Links ◽  
Ionic Hydrogen Bonds ◽  
Chlorobutyl Rubber

ABSTRACT Thermoreversible cross-linking polymers are designed based on reversible cross-linking bonds. These bonds are able to reversibly dissociate and associate upon the input of external energy, such as heat or light. Reprocessibility is possible for this kind of material. The objective was to thermoreversibly cross-link maleic anhydride grafted chlorobutyl rubber (MAH-g-CIIR) via a reaction with octadecylamine, with an excess to obtain amide-salts, which form both hydrogen bonds and ionic interactions. X-ray diffraction experiments showed the presence of microphase-separated aggregates that acted as physical cross-links for both the MAH-g-CIIR precursor and amide-salts. The tensile properties were improved by converting MAH-g-CIIR to amide-salts, because of the combination of hydrogen bonding and ionic interactions. The cross-linked materials could be repeatedly compression molded at 155 °C into homogeneous films. The differential scanning calorimetry curves and Fourier transform infrared spectra indicate that hydrogen bonds are of a thermoreversible nature, but the recovery of ionic bonds is impossible. After treatment with heating-cooling for up to three cycles, the tensile strength of the thermoreversible cross-linking CIIR was greatly reduced. The gradual reduction in the effectiveness of the ionic-hydrogen bonds is the major contribution to the reprocessibility of these materials.

scholarly journals Immobilized artificial membrane (IAM) liquid chromatography as a model for antimicrobial peptide partitioning into cell membranes: An evaluation

Eureka ◽  
2010 ◽  
Vol 1 (1) ◽  
pp. 20-33
Author(s):  
Matthew Benesch ◽  
Ruthvnen Lewis ◽  
Ronald McElhaney
Keyword(s):  
Liquid Chromatography ◽  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Screening Method ◽  
Interfacial Region ◽  
Artificial Membrane ◽  
Lipid Packing ◽  
Immobilized Artificial Membrane ◽  
Fast Screening ◽  
Packing Densities

Non-covalent immobilized artificial membrane reverse-phase high performance liquid chromatography was previously evaluated as a means whereby elution times for antimicrobial peptides from columns mimicking the lipid bilayers of different membrane systems might be used as a fast-screening method to compare relative binding effectiveness. Such a system would aid in the development of antimicrobial peptides that bind preferentially to model pathogenic systems and leave the host’s membranes reasonably unaffected. A non-covalent approach allows for flexibility in membrane composition but was found to be inadequate for analysis of most peptides due to significant lipid loss at high acetonitrile concentrations. A covalent approach where phosphatidylcholine was amide-linked to the silica surface was examined to evaluate its use as a fast-screening method and compare its data to that collected from the non-covalent columns. Initial work with a 1-cm column proved ineffective due to problems with balancing flow rates with retention times, and work was shifted to a longer 10-cm column. Results suggested that peptides bind much more strongly to covalent columns than non-covalent ones, with the binding especially enhanced by the presence of cationic residues. These columns had lipid packing densities much lower than true membranes, indicating that the peptides were partitioning deep into the bonded phase of the columns rather than into the interfacial region of the phosphate head groups, as expected in situations of biologically-relevant lipid packing densities.

scholarly journals Methyl-branched lipids promote the membrane adsorption of α-synuclein by enhancing shallow lipid-packing defects

2015 ◽  
Vol 17 (24) ◽  
pp. 15589-15597 ◽  
Author(s):  
Matthias Garten ◽  
Coline Prévost ◽  
Clotilde Cadart ◽  
Romain Gautier ◽  
Luc Bousset ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Alpha Synuclein ◽  
Giant Unilamellar Vesicles ◽  
Unilamellar Vesicles ◽  
Lipid Packing ◽  
Packing Defects ◽  
Dynamics Simulations ◽  
Flat Membranes

Reconstitution experiments on Giant Unilamellar Vesicles and Molecular Dynamics Simulations indicate that alpha-synuclein binds to neutral flat membranes in the presence of methyl-branched lipids.

Characterization of Doubly Ionic Hydrogen Bonds in Protic Ionic Liquids by NMR Deuteron Quadrupole Coupling Constants: Differences to H-bonds in Amides, Peptides, and Proteins

2017 ◽  
Vol 56 (45) ◽  
pp. 14310-14314 ◽  
Author(s):  
Alexander E. Khudozhitkov ◽  
Peter Stange ◽  
Benjamin Golub ◽  
Dietmar Paschek ◽  
Alexander G. Stepanov ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Hydrogen Bonds ◽  
Coupling Constants ◽  
Protic Ionic Liquids ◽  
Quadrupole Coupling ◽  
Ionic Hydrogen Bonds
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