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

Result code in 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>
Result on the web
<a href="http://www.interdisciplinarymeeting.cz/" target="_blank" >http://www.interdisciplinarymeeting.cz/</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
ROLE OF PROLINE/GLYCINE KINK IN PORE FORMATION BY ANTIMICROBIAL PEPTIDES
Original language description
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.
Czech name
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Czech description
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Project
<a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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