ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00118418" target="_blank" >RIV/00216224:14740/20:00118418 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.interdisciplinarymeeting.cz/" target="_blank" >http://www.interdisciplinarymeeting.cz/</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES

Popis výsledku v původním jazyce

Antimicrobial peptides (AMPs) can selectively disrupt bacterial membranes by the formation of leaky pores (see Fig. 1). Their selectivity and potency make them an appealing subject for drug development. Unfortunately, matching the peptide properties with their activity remains elusive. For instance, the role of proline/glycine kink in alfa-helical peptides was reported to both enhance and reduce the antimicrobial activity. In this work, we combined molecular dynamics simulations and fluorescence leakage assays to demonstrate that a helical kink stabilizes toroidal pores but disrupts barrel-stave pores. In addition, the exact position of the proline/glycine kink in the peptide sequence further controls the structure of toroidal pores. The provided molecular-level insight could be utilized for the design and modification of pore-forming antibacterial peptides.

Název v anglickém jazyce

ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES

Popis výsledku anglicky

Antimicrobial peptides (AMPs) can selectively disrupt bacterial membranes by the formation of leaky pores (see Fig. 1). Their selectivity and potency make them an appealing subject for drug development. Unfortunately, matching the peptide properties with their activity remains elusive. For instance, the role of proline/glycine kink in alfa-helical peptides was reported to both enhance and reduce the antimicrobial activity. In this work, we combined molecular dynamics simulations and fluorescence leakage assays to demonstrate that a helical kink stabilizes toroidal pores but disrupts barrel-stave pores. In addition, the exact position of the proline/glycine kink in the peptide sequence further controls the structure of toroidal pores. The provided molecular-level insight could be utilized for the design and modification of pore-forming antibacterial peptides.

Druh

O - Ostatní výsledky

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2020

Kód důvěrnosti údajů

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