Interaction of amphipathic -helical peptides with a lipid membrane: Adsorption and pore formation

2014 ◽  
Vol 401 ◽  
pp. 45-51 ◽  
Author(s):  
Vladimir P. Zhdanov
Keyword(s):  
Pore Formation ◽  
Lipid Membrane ◽  
Helical Peptides

Dimerization of the Antimicrobial Peptide Polyphemusin I into One Polypeptide Chain: Theoretical and Practical Consequences

2019 ◽  
Vol 35 (5) ◽  
pp. 36-41
Author(s):  
V.A. Zenin ◽  
E.G. Sadykhov ◽  
A.N. Fedorov
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Lipid Membrane ◽  
Polypeptide Chain ◽  
Unique Identifier ◽  
Bacterial Cultures ◽  
In Series ◽  
The Russian Federation ◽  
Peptide Dimerization ◽  
Putative Mechanism

A strategy of sequential dimerization of monomers of antimicrobial peptides (AMPs) into one polypeptide chain has been implemented on the example of a beta-structural AMP polyphemusin I which is one of the most effective candidate for use as an antibiotic. The possible polyphemusin I monomer and dimer structures in lipid membrane were studied in this work via molecular modeling. To this end, these molecules were chemically synthesized so that the dimer represented two monomers connected in series into one polypeptide chain with a flexible linker. The antimicrobial effects of monomer and dimer were then tested on various bacterial cultures, and their similarity was shown. Therefore, we can conclude that the pore formation is not a putative mechanism of the polyphemusin I action. antimicrobial peptides, peptide dimerization, mechanism of antimicrobial action, polyphemusin The work was supported by the Ministry of Science and Higher Education of the Russian Federation (Project Unique Identifier RFMEFI57517X0151).

scholarly journals Proof of pore formation and biophysical perturbations through a 2D amoxicillin-lipid membrane interaction approach

2017 ◽  
Vol 1859 (5) ◽  
pp. 803-812 ◽  
Author(s):  
Daniela Lopes ◽  
Cláudia Nunes ◽  
Philippe Fontaine ◽  
Bruno Sarmento ◽  
Salette Reis
Keyword(s):  
Pore Formation ◽  
Lipid Membrane ◽  
Membrane Interaction ◽  
Interaction Approach

scholarly journals Pore formation in lipid membrane II: Energy landscape under external stress

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Sergey A. Akimov ◽  
Pavel E. Volynsky ◽  
Timur R. Galimzyanov ◽  
Peter I. Kuzmin ◽  
Konstantin V. Pavlov ◽  
...  
Keyword(s):  
Pore Formation ◽  
Lipid Membrane ◽  
Energy Landscape ◽  
External Stress

scholarly journals Lipid II-Mediated Pore Formation by the Peptide Antibiotic Nisin: a Black Lipid Membrane Study

2004 ◽  
Vol 186 (10) ◽  
pp. 3259-3261 ◽  
Author(s):  
Imke Wiedemann ◽  
Roland Benz ◽  
Hans-Georg Sahl
Keyword(s):  
Cell Wall ◽  
Pore Formation ◽  
Cytoplasmic Membrane ◽  
Lipid Membrane ◽  
Specific Interaction ◽  
Peptide Antibiotic ◽  
Black Lipid Membrane ◽  
Lipid Ii ◽  
Antibiotic Peptide

ABSTRACT The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.

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 Molecular Dynamics Simulations of the Permeation of Bisphenol A and Pore Formation in a Lipid Membrane

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Liang Chen ◽  
Junlang Chen ◽  
Guoquan Zhou ◽  
Yu Wang ◽  
Can Xu ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Bisphenol A ◽  
Molecular Dynamics Simulations ◽  
Pore Formation ◽  
Lipid Membrane ◽  
Dynamics Simulations

scholarly journals Pore formation in lipid membrane I: Continuous reversible trajectory from intact bilayer through hydrophobic defect to transversal pore

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Sergey A. Akimov ◽  
Pavel E. Volynsky ◽  
Timur R. Galimzyanov ◽  
Peter I. Kuzmin ◽  
Konstantin V. Pavlov ◽  
...  
Keyword(s):  
Pore Formation ◽  
Lipid Membrane

Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation

2004 ◽  
Vol 34 (3) ◽  
pp. 230-242 ◽  
Author(s):  
Assaf Zemel ◽  
Avinoam Ben-Shaul ◽  
Sylvio May
Keyword(s):  
Pore Formation ◽  
Lipid Membrane ◽  
Amphipathic Peptides

Mechanics of water pore formation in lipid membrane under electric field

2017 ◽  
Vol 33 (2) ◽  
pp. 234-242 ◽  
Author(s):  
Bing Bu ◽  
Dechang Li ◽  
Jiajie Diao ◽  
Baohua Ji
Keyword(s):  
Electric Field ◽  
Pore Formation ◽  
Lipid Membrane ◽  
Water Pore

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.

Sign in / Sign up

Export Citation Format

Share Document