Effect of helical kink in antimicrobial peptides on membrane
pore formation

J 2020

Effect of helical kink in antimicrobial peptides on membrane pore formation

TÜRKOVÁ, Alžběta, Ivo KABELKA, Tereza KRÁLOVÁ, Lukáš SUKENÍK, Šárka POKORNÁ et. al.

Basic information

Original name

Effect of helical kink in antimicrobial peptides on membrane pore formation

Authors

TÜRKOVÁ, Alžběta (203 Czech Republic, belonging to the institution), Ivo KABELKA (203 Czech Republic, belonging to the institution), Tereza KRÁLOVÁ (203 Czech Republic, belonging to the institution), Lukáš SUKENÍK (203 Czech Republic, belonging to the institution), Šárka POKORNÁ, Martin HOF and Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution)

Edition

eLife, Cambridge, eLife Sciences Publications Ltd, 2020, 2050-084X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10403 Physical chemistry

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 8.140

RIV identification code

RIV/00216224:14740/20:00114711

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.7554/eLife.47946

UT WoS

000519949800001

Keywords in English

Melitten; Magainins; Polypeptide Antibiotic Agent

Abstract

V originále

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.

Links

GA17-11571S, research and development project

Name: Amfifilní peptidy na fosfolipidových membránách

Investor: Czech Science Foundation

LM2015085, research and development project

Name: CERIT Scientific Cloud (Acronym: CERIT-SC)

Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

90070, large research infrastructures

Name: IT4Innovations

Citovat

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.

@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.

Detailed Information on Publication Record