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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