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

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 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 Enhanced Membrane Pore Formation through High-Affinity Targeted Antimicrobial Peptides

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39768 ◽  
Author(s):  
Christopher J. Arnusch ◽  
Roland J. Pieters ◽  
Eefjan Breukink
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Membrane Pore ◽  
High Affinity

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.

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).

Membrane pore formation at protein–lipid interfaces

2014 ◽  
Vol 39 (11) ◽  
pp. 510-516 ◽  
Author(s):  
Robert J.C. Gilbert ◽  
Mauro Dalla Serra ◽  
Christopher J. Froelich ◽  
Mark I. Wallace ◽  
Gregor Anderluh
Keyword(s):  
Pore Formation ◽  
Membrane Pore

scholarly journals Molecular Basis for Membrane Pore Formation by Bax Protein Carboxyl Terminus

Biochemistry ◽  
2012 ◽  
Vol 51 (46) ◽  
pp. 9406-9419 ◽  
Author(s):  
Suren A. Tatulian ◽  
Pranav Garg ◽  
Kathleen N. Nemec ◽  
Bo Chen ◽  
Annette R. Khaled
Keyword(s):  
Molecular Basis ◽  
Pore Formation ◽  
Carboxyl Terminus ◽  
Membrane Pore ◽  
Bax Protein
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