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H1 helix of colicin U causes phospholipid membrane permeation

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F22%3A00552507" target="_blank" >RIV/61388955:_____/22:00552507 - isvavai.cz</a>

  • Nalezeny alternativní kódy

    RIV/00216208:11310/22:10447275

  • Výsledek na webu

    <a href="http://hdl.handle.net/11104/0327618" target="_blank" >http://hdl.handle.net/11104/0327618</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbamem.2022.183866" target="_blank" >10.1016/j.bbamem.2022.183866</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    H1 helix of colicin U causes phospholipid membrane permeation

  • Popis výsledku v původním jazyce

    In light of an increasing number of antibiotic-resistant bacterial strains, it is essential to understand an action imposed by various antimicrobial agents on bacteria at the molecular level. One of the leading mechanisms of killing bacteria is related to the alteration of their plasmatic membrane. We study bio-inspired peptides originating from natural antimicrobial proteins colicins, which can disrupt membranes of bacterial cells. Namely, we focus on the α-helix H1 of colicin U, produced by bacterium Shigella boydii, and compare it with analogous peptides derived from two different colicins. To address the behavior of the peptides in biological membranes, we employ a combination of molecular simulations and experiments. We use molecular dynamics simulations to show that all three peptides are stable in model zwitterionic and negatively charged phospholipid membranes. At the molecular level, their embedment leads to the formation of membrane defects, membrane permeation for water, and, for negatively charged lipids, membrane poration. These effects are caused by the presence of polar moieties in the considered peptides. Importantly, simulations demonstrate that even monomeric H1 peptides can form toroidal pores. At the macroscopic level, we employ experimental co-sedimentation and fluorescence leakage assays. We show that the H1 peptide of colicin U incorporates into phospholipid vesicles and disrupts their membranes, causing leakage, in agreement with the molecular simulations. These insights obtained for model systems seem important for understanding the mechanisms of antimicrobial action of natural bacteriocins and for future exploration of small bio-inspired peptides able to disrupt bacterial membranes.

  • Název v anglickém jazyce

    H1 helix of colicin U causes phospholipid membrane permeation

  • Popis výsledku anglicky

    In light of an increasing number of antibiotic-resistant bacterial strains, it is essential to understand an action imposed by various antimicrobial agents on bacteria at the molecular level. One of the leading mechanisms of killing bacteria is related to the alteration of their plasmatic membrane. We study bio-inspired peptides originating from natural antimicrobial proteins colicins, which can disrupt membranes of bacterial cells. Namely, we focus on the α-helix H1 of colicin U, produced by bacterium Shigella boydii, and compare it with analogous peptides derived from two different colicins. To address the behavior of the peptides in biological membranes, we employ a combination of molecular simulations and experiments. We use molecular dynamics simulations to show that all three peptides are stable in model zwitterionic and negatively charged phospholipid membranes. At the molecular level, their embedment leads to the formation of membrane defects, membrane permeation for water, and, for negatively charged lipids, membrane poration. These effects are caused by the presence of polar moieties in the considered peptides. Importantly, simulations demonstrate that even monomeric H1 peptides can form toroidal pores. At the macroscopic level, we employ experimental co-sedimentation and fluorescence leakage assays. We show that the H1 peptide of colicin U incorporates into phospholipid vesicles and disrupts their membranes, causing leakage, in agreement with the molecular simulations. These insights obtained for model systems seem important for understanding the mechanisms of antimicrobial action of natural bacteriocins and for future exploration of small bio-inspired peptides able to disrupt bacterial membranes.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10403 - Physical chemistry

Návaznosti výsledku

  • Projekt

    <a href="/cs/project/GA18-26751S" target="_blank" >GA18-26751S: Penetrace, akumulace a interakce vybraných modelových léčiv s modelovou lipidovou vrstvou slzného filmu utvářejícího se na povrchu lidského oka</a><br>

  • Návaznosti

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Ostatní

  • Rok uplatnění

    2022

  • Kód důvěrnosti údajů

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Údaje specifické pro druh výsledku

  • Název periodika

    Biochimica Et Biophysica Acta-Biomembranes

  • ISSN

    0005-2736

  • e-ISSN

    1879-2642

  • Svazek periodika

    1864

  • Číslo periodika v rámci svazku

    4

  • Stát vydavatele periodika

    NL - Nizozemsko

  • Počet stran výsledku

    10

  • Strana od-do

    183866

  • Kód UT WoS článku

    000788113600010

  • EID výsledku v databázi Scopus

    2-s2.0-85122953244