Lipid Bilayers: Structure, Dynamics, and Interactions with Antimicrobial Peptides

2014 ◽  
pp. 212-237
Keyword(s):  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Structure Dynamics

Heterodimer Formation between the Antimicrobial Peptides Magainin 2 and PGLa in Lipid Bilayers:  A Cross-Linking Study†

Biochemistry ◽  
2001 ◽  
Vol 40 (41) ◽  
pp. 12395-12399 ◽  
Author(s):  
Toshiaki Hara ◽  
Yasuyuki Mitani ◽  
Kyoko Tanaka ◽  
Natsuko Uematsu ◽  
Asako Takakura ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Cross Linking

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 Morphological Changes Induced by the Action of Antimicrobial Peptides on Supported Lipid Bilayers

2011 ◽  
Vol 115 (1) ◽  
pp. 158-167 ◽  
Author(s):  
Ahmad Arouri ◽  
Volker Kiessling ◽  
Lukas Tamm ◽  
Margitta Dathe ◽  
Alfred Blume
Keyword(s):  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Morphological Changes ◽  
Supported Lipid Bilayers

scholarly journals Curved Lipid Bilayers: Structure, Dynamics, Phase Properties and Surface Electrostatics

2014 ◽  
Vol 106 (2) ◽  
pp. 221a
Author(s):  
Antonin Marek ◽  
Amir Koolivand ◽  
David Song ◽  
Maxim A. Voinov ◽  
Alex I. Smirnov
Keyword(s):  
Lipid Bilayers ◽  
Structure Dynamics ◽  
Phase Properties

scholarly journals Lysylated phospholipids stabilize models of bacterial lipid bilayers and protect against antimicrobial peptides

2014 ◽  
Vol 1838 (9) ◽  
pp. 2198-2204 ◽  
Author(s):  
Elizabeth Cox ◽  
Austen Michalak ◽  
Sarah Pagentine ◽  
Pamela Seaton ◽  
Antje Pokorny
Keyword(s):  
Antimicrobial Peptides ◽  
Lipid Bilayers ◽  
Bacterial Lipid

Synergistic effects of magainin 2 and PGLa on their heterodimer formation, aggregation, and insertion into the bilayer

RSC Advances ◽  
2015 ◽  
Vol 5 (3) ◽  
pp. 2047-2055 ◽  
Author(s):  
Eol Han ◽  
Hwankyu Lee
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptides ◽  
Molecular Dynamics Simulations ◽  
Lipid Bilayers ◽  
Synergistic Effects ◽  
Coarse Grained ◽  
Dynamics Simulations ◽  
Coarse Grained Molecular Dynamics

We performed coarse-grained molecular dynamics simulations of antimicrobial peptides PGLa and magainin 2 in lipid bilayers.

scholarly journals Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles

2021 ◽  
Author(s):  
Yevhen K. Cherniavskyi ◽  
Rosario Oliva ◽  
Marco Stellato ◽  
Pompea Del Vecchio ◽  
Stefania Galdiero ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptides ◽  
Molecular Dynamics Simulations ◽  
Lipid Bilayers ◽  
Structural Characterization ◽  
Bacterial Membrane ◽  
Membrane Composition ◽  
Membrane Mimetic ◽  
Dynamics Simulations

Antimicrobial peptides are a promising class of alternative antibiotics that interact selectively with negatively charged lipid bilayers. This paper presents the structural characterization of the antimicrobial peptides myxinidin and WMR associated with bacterial membrane mimetic micelles and bicelles by NMR, CD spectroscopy, and Molecular Dynamics simulations. Both peptides adopt a different conformation in the lipidic environment than in aqueous solution. The location of peptides in micelles and bicelles has been studied by paramagnetic relaxation enhancement experiments with paramagnetic tagged 5- and 16-doxyl stearic acid (5-/16-SASL). Multi-microsecond long molecular dynamics simulations of multiple copies of the peptides were used to gain an atomic level of detail on membrane-peptide and peptide-peptide interactions. Our results highlight an essential role of the negatively charged membrane mimetic in the structural stability of both myxinidin and WMR. The peptides localize predominantly in the membrane's headgroup region and have a noticeable membrane thinning effect on the overall bilayer structure. Myxinidin and WMR show different tendency to self-aggregate, which is also influenced by the membrane composition (DOPE/DOPG versus DOPE/DOPG/CL) and can be related to the previously observed difference in the ability of the peptides to disrupt different types of model membranes.

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