| TÜRKOVÁ, Alžběta, Ivo KABELKA, Tereza KRÁLOVÁ, Lukáš SUKENÍK, Šárka POKORNÁ, Martin HOF and Robert VÁCHA. Effect of helical kink in antimicrobial peptides on membrane pore formation. eLife. Cambridge: eLife Sciences Publications Ltd, 2020, vol. 9, March 2020, p. 1-38. ISSN 2050-084X. Available from: https://dx.doi.org/10.7554/eLife.47946. |
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@article{1731416,
author = {Türková, Alžběta and Kabelka, Ivo and Králová, Tereza and Sukeník, Lukáš and Pokorná, Šárka and Hof, Martin and Vácha, Robert},
article_location = {Cambridge},
article_number = {March 2020},
doi = {http://dx.doi.org/10.7554/eLife.47946},
keywords = {Melitten; Magainins; Polypeptide Antibiotic Agent},
language = {eng},
issn = {2050-084X},
journal = {eLife},
title = {Effect of helical kink in antimicrobial peptides on membrane pore formation},
url = {https://elifesciences.org/articles/47946},
volume = {9},
year = {2020}
}
TY - JOUR
ID - 1731416
AU - Türková, Alžběta - Kabelka, Ivo - Králová, Tereza - Sukeník, Lukáš - Pokorná, Šárka - Hof, Martin - Vácha, Robert
PY - 2020
TI - Effect of helical kink in antimicrobial peptides on membrane pore formation
JF - eLife
VL - 9
IS - March 2020
SP - 1-38
EP - 1-38
PB - eLife Sciences Publications Ltd
SN - 2050084X
KW - Melitten
KW - Magainins
KW - Polypeptide Antibiotic Agent
UR - https://elifesciences.org/articles/47946
L2 - https://elifesciences.org/articles/47946
N2 - Every cell is protected by a semipermeable membrane. Peptides with the rightproperties, for example Antimicrobial peptides (AMPs), can disrupt this protective barrier byformation of leaky pores. Unfortunately, matching peptide properties with their ability toselectively form pores in bacterial membranes remains elusive. In particular, the proline/glycine kinkin helical peptides was reported to both increase and decrease antimicrobial activity. We usedcomputer simulations and fluorescence experiments to show that a kink in helices affects theformation of membrane pores by stabilizing toroidal pores but disrupting barrel-stave pores. Theposition of the proline/glycine kink in the sequence further controls the specific structure oftoroidal pore. Moreover, we demonstrate that two helical peptides can form a kink-like connectionwith similar behavior as one long helical peptide with a kink. The provided molecular-level insightcan be utilized for design and modification of pore-forming antibacterial peptides or toxins.
ER -
TÜRKOVÁ, Alžběta, Ivo KABELKA, Tereza KRÁLOVÁ, Lukáš SUKENÍK, Šárka POKORNÁ, Martin HOF and Robert VÁCHA. Effect of helical kink in antimicrobial peptides on membrane pore formation. \textit{eLife}. Cambridge: eLife Sciences Publications Ltd, 2020, vol.~9, March 2020, p.~1-38. ISSN~2050-084X. Available from: https://dx.doi.org/10.7554/eLife.47946.
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