Extension of the CAVS model to helical peptides in membrane environment

2021 ◽  
Author(s):  
Hujun Shen ◽  
Zhenhua Wu ◽  
Chan Lu
Keyword(s):  
Lipid Membrane ◽  
Dipole Potential ◽  
Helical Peptides ◽  
Helical Peptide ◽  
Peptide Insertion

Considering the effect of peptide insertion on the dipole potential of lipid membrane, we extend the CAVS coarse-gained (CG) model to the simulation of helical peptide in membrane environment. In...

scholarly journals Amphipathic helical peptide-based fluorogenic probes for a marker-free analysis of exosomes based on membrane-curvature sensing

RSC Advances ◽  
2020 ◽  
Vol 10 (63) ◽  
pp. 38323-38327
Author(s):  
Yusuke Sato ◽  
Kazuki Kuwahara ◽  
Kenta Mogami ◽  
Kenta Takahashi ◽  
Seiichi Nishizawa
Keyword(s):  
Membrane Curvature ◽  
Helical Peptides ◽  
Curvature Sensing ◽  
Helical Peptide ◽  
Fluorogenic Probes ◽  
Marker Free

Fluorogenic probes based on membrane curvature sensing-amphipathic helical peptides have been developed for a marker-free exosome analysis.

scholarly journals Modulation of host lipid membrane elasticity and dipole potential induced by bacterial membrane vesicles

2019 ◽  
Author(s):  
Ashutosh Prince ◽  
Anuj Tiwari ◽  
Titas Mandal ◽  
Kuldeep Sharma ◽  
Nikhil Kanik ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Lipid Membranes ◽  
Lipid Membrane ◽  
Membrane Vesicles ◽  
Bacterial Membrane ◽  
Dipole Potential ◽  
Long Distance ◽  
Biologically Relevant ◽  
Host Membrane ◽  
Distance Delivery

AbstractBacterial membrane vesicles (MVs) facilitate long-distance delivery of virulence factors crucial for pathogenicity. The entry and trafficking mechanisms of virulence factors inside host cells is recently emerging, however, if bacterial MVs modulate the physicochemical properties of the host lipid membrane remains unknown. Here we reconstitute the interaction of bacterial MV with host cell lipid membranes and quantitatively show that bacterial MV interaction increases the fluidity, dipole potential and elasticity of a biologically relevant multi-component host membrane. The presence of cylindrical lipids such as phosphatidylcholine and phosphatidylinositol and a moderate acyl chain length of C16 helps the MV interaction. While significant binding of bacterial MVs to the raft-like lipid membranes with phase separated regions of the membrane was observed, however, MVs have a preference for binding to the liquid disordered regions of the membrane. Further, the elevated levels of cholesterol tend to hinder the interaction of bacterial MVs. We further quantify the change in excess Gibbs free energy of mixing of bacterial MVs with host lipid membranes driving the modulation of host membrane parameters. The findings may have significant implications on the regulation of host machineries by pathogen through manipulation of host membrane properties.Significance StatementBacterial membrane vesicles (MVs) act as the long-distance delivery tools for virulence factor and thus, directly implicated in host-pathogen interactions and pathogenicity. While the mechanisms of virulence transfer is only recently emerging, however, the interaction of MVs the host cell membrane remains largely unexplored. Whether the MVs interaction can locally modulate the host lipid membrane physicochemical properties (such as fluidity, dipole potential and elasticity) remains unknown. Here, we quantitatively investigate the lipid specificity of E. Coli MV interaction and this results in increase in the fluidity, dipole potential and in-plane elasticity of a biologically relevant multi-component host membrane. The findings could be important for numerous cell-signaling processes as well as downstream events involving membrane-membrane fusion during process of phagosome maturation.

Effect of oscillation dynamics on long-range electron transfer in a helical peptide monolayer

2018 ◽  
Vol 20 (22) ◽  
pp. 15216-15222 ◽  
Author(s):  
Daisuke Matsushita ◽  
Hirotaka Uji ◽  
Shunsaku Kimura
Keyword(s):  
Electron Transfer ◽  
Long Range ◽  
Self Assembled Monolayers ◽  
Helical Peptides ◽  
Helical Peptide ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Oscillation Dynamics

Electron transfer (ET) reactions via helical peptides composed of –(Aib-Pro)n– were studied in self-assembled monolayers and compared with –(Ala-Aib)n– peptides.

scholarly journals Impact of Dehydroamino Acids on the Structure and Stability of Incipient 3₁₀ Helical Peptides

2019 ◽  
Author(s):  
Daniel Joaquin ◽  
Michael A. Lee ◽  
David W. Kastner ◽  
Jatinder Singh ◽  
Shardon T. Morrill ◽  
...  
Keyword(s):  
Room Temperature ◽  
Bioactive Peptides ◽  
Elevated Temperatures ◽  
Peptide Structure ◽  
Helical Peptides ◽  
Dehydroamino Acids ◽  
Structure And Stability ◽  
Helical Peptide ◽  
Proteolytic Stability ◽  
The Impact

<div>A comparative study of the impact of small, medium-sized, and bulky Δ,Δ-dehydroamino acids (ΔAAs) on the structure and stability of Balaram’s incipient 3₁₀ -helical peptide (1) is reported. Replacement of the N-terminal Aib residue of 1 with a ΔAA afforded peptides 2a–c that maintained the 310-helical shape of 1 in solution. In contrast, installation of a ΔAA in place of Aib-3 yielded peptides 3a–c that preferred a Δ-sheet-like conformation. The impact of the ΔAA on peptide structure was independent of size, with small (ΔAla), medium-sized (Z-ΔAbu), and bulky (ΔVal) ΔAAs exerting similar effects. The proteolytic stabilities of 1 and its analogs were determined by incubation with Pronase. Z-ΔAbu and ΔVal increased the resistance of peptides to proteolysis when incorporated at the 3-position and had negligible impact on stability when placed at the 1-position, whereas ΔAla-containing peptides degraded rapidly regardless of position. Exposure of peptides 2a–c and 3a–c to the reactive thiol cysteamine revealed that ΔAla-containing peptides underwent conjugate addition at room temperature, while Z-ΔAbu- and ΔVal-containing peptides were inert even at elevated temperatures. These results suggest that both bulky and the more synthetically accessible medium-sized ΔAAs should be valuable tools for bestowing rigidity and proteolytic stability on bioactive peptides.</div>

scholarly journals Effect of helical kink in antimicrobial peptides on membrane pore formation

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Alzbeta Tuerkova ◽  
Ivo Kabelka ◽  
Tereza Králová ◽  
Lukáš Sukeník ◽  
Šárka Pokorná ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Molecular Level ◽  
Helical Peptides ◽  
Membrane Pore ◽  
Bacterial Membranes ◽  
Membrane Pores ◽  
Helical Peptide ◽  
Toroidal Pore ◽  
The Right

Every cell is protected by a semipermeable membrane. Peptides with the right properties, for example Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore-forming antibacterial peptides or toxins.

scholarly journals Impact of Dehydroamino Acids on the Structure and Stability of Incipient 3₁₀ Helical Peptides

2019 ◽  
Author(s):  
Daniel Joaquin ◽  
Michael A. Lee ◽  
David W. Kastner ◽  
Jatinder Singh ◽  
Shardon T. Morrill ◽  
...  
Keyword(s):  
Room Temperature ◽  
Bioactive Peptides ◽  
Elevated Temperatures ◽  
Peptide Structure ◽  
Helical Peptides ◽  
Dehydroamino Acids ◽  
Structure And Stability ◽  
Helical Peptide ◽  
Proteolytic Stability ◽  
The Impact

<div>A comparative study of the impact of small, medium-sized, and bulky Δ,Δ-dehydroamino acids (ΔAAs) on the structure and stability of Balaram’s incipient 3₁₀ -helical peptide (1) is reported. Replacement of the N-terminal Aib residue of 1 with a ΔAA afforded peptides 2a–c that maintained the 310-helical shape of 1 in solution. In contrast, installation of a ΔAA in place of Aib-3 yielded peptides 3a–c that preferred a Δ-sheet-like conformation. The impact of the ΔAA on peptide structure was independent of size, with small (ΔAla), medium-sized (Z-ΔAbu), and bulky (ΔVal) ΔAAs exerting similar effects. The proteolytic stabilities of 1 and its analogs were determined by incubation with Pronase. Z-ΔAbu and ΔVal increased the resistance of peptides to proteolysis when incorporated at the 3-position and had negligible impact on stability when placed at the 1-position, whereas ΔAla-containing peptides degraded rapidly regardless of position. Exposure of peptides 2a–c and 3a–c to the reactive thiol cysteamine revealed that ΔAla-containing peptides underwent conjugate addition at room temperature, while Z-ΔAbu- and ΔVal-containing peptides were inert even at elevated temperatures. These results suggest that both bulky and the more synthetically accessible medium-sized ΔAAs should be valuable tools for bestowing rigidity and proteolytic stability on bioactive peptides.</div>

scholarly journals Effect of Helical Kink in Antimicrobial Peptides on Membrane Pore Formation

2019 ◽  
Author(s):  
Alzbeta Tuerkova ◽  
Ivo Kabelka ◽  
Tereza Králová ◽  
Lukáš Sukeník ◽  
Šárka Pokorná ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Molecular Level ◽  
Helical Peptides ◽  
Membrane Pore ◽  
Bacterial Membranes ◽  
Membrane Pores ◽  
Helical Peptide ◽  
Toroidal Pore ◽  
The Right

AbstractEvery cell is protected by a semipermeable membrane. Peptides with the right properties, e.g. Antimicrobial peptides (AMPs), can disrupt this protective barrier by formation of leaky pores. Unfortunately, matching peptide properties with their ability to selectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kink in helical peptides was reported to both increase and decrease antimicrobial activity. We used computer simulations and fluorescence experiments to show that a kink in helices affects the formation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. The position of the proline/glycine kink in the sequence further controls the specific structure of toroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connection with similar behavior as one long helical peptide with a kink. The provided molecular-level insight can be utilized for design and modification of pore forming antibacterial peptides or toxins.

A virtual instrumentation based protocol for the automated implementation of the inner field compensation method

Open Physics ◽  
2006 ◽  
Vol 4 (3) ◽  
Author(s):  
Loredana Mereuta ◽  
Tudor Luchian
Keyword(s):  
Transmembrane Potential ◽  
Lipid Membrane ◽  
Cell Physiology ◽  
Dipole Potential ◽  
Virtual Instrumentation ◽  
Electrical Parameters ◽  
Membrane Dipole Potential ◽  
Membrane Bound ◽  
The Difference ◽  
Extracellular Ions

AbstractOne influential parameter which mediates interactions between many types of molecules and biological membranes stems from the lumped contributions of the transmembrane potential, dipole potential and the difference in the surface potentials on both sides of a membrane. With relevance to cell physiology, such electrical features of a biomembrane are prone to undergoing changes as a result of interactions with the aqueous surrounding. Among the most useful tools devoted to exploring changes of electrical parameters of a lipid membrane induced by certain extracellular ions, lipid composition, and embedded membrane peptides and proteins, are spectroscopic imaging and the inner field compensation (IFC) method. In this work we layout the principles of a fully computerized version of the IFC method, which makes it more readily available to users. As a direct application, we deployed this improved version of the IFC method to time-resolve changes induced by alamethicin monomers upon membrane dipole potential, following their aggregation within an artificial lipid membrane. Intriguingly, even prior crossing the membrane core, the membrane-bound alamethicin monomers are shown to significantly increase the dipole potential of the monolayer they reside in. Such data further emphasize the yet less-explored interplay between membrane-based protein and peptides, and the membrane dipole potential.

scholarly journals Probing the Lipid Membrane Dipole Potential by Atomic Force Microscopy

2008 ◽  
Vol 95 (11) ◽  
pp. 5193-5199 ◽  
Author(s):  
Yi Yang ◽  
Kathryn M. Mayer ◽  
Nissanka S. Wickremasinghe ◽  
Jason H. Hafner
Keyword(s):  
Atomic Force Microscopy ◽  
Lipid Membrane ◽  
Dipole Potential ◽  
Membrane Dipole Potential ◽  
Force Microscopy ◽  
Atomic Force
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