Electrochemical and AFM study of the interaction of recombinant human cathelicidin LL-37 with various supported bilayer lipid membranes

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F18%3A00490127" target="_blank" >RIV/61388955:_____/18:00490127 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.jelechem.2018.01.019" target="_blank" >http://dx.doi.org/10.1016/j.jelechem.2018.01.019</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jelechem.2018.01.019" target="_blank" >10.1016/j.jelechem.2018.01.019</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electrochemical and AFM study of the interaction of recombinant human cathelicidin LL-37 with various supported bilayer lipid membranes

Popis výsledku v původním jazyce

The overuse of antibiotics is strongly associated with the development of the bacterial resistance which means that novel antimicrobial agents with different mode of action must be prepared. Antimicrobial peptides (AMP) can serve as almost an ideal candidate for the new generation of antimicrobial compounds. In this work the interactions of recombinantly prepared cathelicidin LL-37 towards various types and mixtures of supported bilayer lipid membranes (s-BLMs) are studied by cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS), and atomic force microscopy (AFM). All of these methods have approved excellent efficiency of LL-37 towards membranes that are typical for prokaryotic organisms composed mainly of phosphatidylglycerol and lipid A. On the contrary, almost zero activity towards phosphatidylcholine membranes that are more frequently found in the structure of eukaryotic organisms was observed. A 'carpet model' where the peptides interact primarily with the lipid head groups, have been proved as a mode of LL-37 action. This finding is based on the results obtained by CV and EIS techniques and was revealed by the visualization of the electrode surface by AFM technique.

Název v anglickém jazyce

Electrochemical and AFM study of the interaction of recombinant human cathelicidin LL-37 with various supported bilayer lipid membranes

Popis výsledku anglicky

The overuse of antibiotics is strongly associated with the development of the bacterial resistance which means that novel antimicrobial agents with different mode of action must be prepared. Antimicrobial peptides (AMP) can serve as almost an ideal candidate for the new generation of antimicrobial compounds. In this work the interactions of recombinantly prepared cathelicidin LL-37 towards various types and mixtures of supported bilayer lipid membranes (s-BLMs) are studied by cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS), and atomic force microscopy (AFM). All of these methods have approved excellent efficiency of LL-37 towards membranes that are typical for prokaryotic organisms composed mainly of phosphatidylglycerol and lipid A. On the contrary, almost zero activity towards phosphatidylcholine membranes that are more frequently found in the structure of eukaryotic organisms was observed. A 'carpet model' where the peptides interact primarily with the lipid head groups, have been proved as a mode of LL-37 action. This finding is based on the results obtained by CV and EIS techniques and was revealed by the visualization of the electrode surface by AFM technique.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Journal of Electroanalytical Chemistry

ISSN

1572-6657

e-ISSN

—

Svazek periodika

821

Číslo periodika v rámci svazku

JUL 2018

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

7

Strana od-do

40-46

Kód UT WoS článku

000437818600007

EID výsledku v databázi Scopus

2-s2.0-85041608981