Ion Pore Formation in Membranes due to Complex Interactions between Lipids and Antimicrobial Peptides or Biomolecules

2012 ◽  
pp. 893-934 ◽  
Author(s):  
Md Ashrafuzzaman ◽  
J Tuszynski
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Complex Interactions ◽  
Ion Pore

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).

Enhanced Membrane Pore Formation by Multimeric/Oligomeric Antimicrobial Peptides†

Biochemistry ◽  
2007 ◽  
Vol 46 (46) ◽  
pp. 13437-13442 ◽  
Author(s):  
Christopher J. Arnusch ◽  
Hilbert Branderhorst ◽  
Ben de Kruijff ◽  
Rob M. J. Liskamp ◽  
Eefjan Breukink ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Membrane Pore

Lipid-dependent pore formation by antimicrobial peptides arenicin-2 and melittin demonstrated by their proton transfer activity

2014 ◽  
Vol 21 (2) ◽  
pp. 71-76 ◽  
Author(s):  
Sergei V. Sychev ◽  
Sergey V. Balandin ◽  
Pavel V. Panteleev ◽  
Leonid I. Barsukov ◽  
Tatiana V. Ovchinnikova
Keyword(s):  
Antimicrobial Peptides ◽  
Proton Transfer ◽  
Pore Formation ◽  
Transfer Activity

scholarly journals Author response: 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 ◽  
Author Response ◽  
Membrane Pore ◽  
Response Effect

scholarly journals Polydiacetylene Vesicles Acting as Colorimetric Sensor for the Detection of Plantaricin LD1 Purified From Lactobacillus Plantarum LD1

2021 ◽  
Author(s):  
Manoj Kumar Yadav ◽  
Santosh Kumar Tiwari
Keyword(s):  
Antimicrobial Peptides ◽  
Lactobacillus Plantarum ◽  
Pore Formation ◽  
Membrane Lipids ◽  
Membrane Disruption ◽  
Target Cells ◽  
Artificial Membrane ◽  
Physiological Processes ◽  
Colorimetric Response ◽  
Pda Vesicles

Abstract The interaction of antimicrobial peptides with membrane lipids plays a major role in numerous physiological processes. Bacteriocins are antimicrobial peptides known to kill target cells by pore formation and membrane disruption. In this study, polydiacetylene (PDA) vesicles were applied as artificial membrane for detection of plantaricin LD1 purified from Lactobacillus plantarum LD1. Plantaricin LD1 (200 µg/ml) was able to change the color of PDA vesicles from blue to red with colorimetric response CR % 30.26 ± 0.59. Nisin (200 µg/ml), used as control, also changed the color of the vesicles with CR % 50.56 ± 0.98 validating the membrane-acting nature of these bacteriocins. The PDA vesicles treated with nisin and plantaricin LD1 showed increased infrared absorbance at 1411.46 cm-1 and 1000-1150 cm-1 indicated the interaction of bacteriocins with phospholipids and fatty acids, respectively. Further, microscopic examination also suggested the disruption of bacteriocin-treated vesicles indicating the interaction of bacteriocins. These findings suggest that the PDA vesicles may be used as bio-mimetic sensor for the detection of bacteriocins produced by several probiotics in food and therapeutic applications.

scholarly journals Membrane Thinning Is Not A Unique Signal Of Pore Formation By Antimicrobial Peptides

2009 ◽  
Vol 96 (3) ◽  
pp. 390a
Author(s):  
Georg Pabst ◽  
Stephan Grage ◽  
Sabine Danner-Pongratz ◽  
Weiguo Jing ◽  
Anne S. Ulrich ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Unique Signal ◽  
Membrane Thinning

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.

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