Kink in Helical Peptides Affects Membrane Pore Formation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F19%3A00112870" target="_blank" >RIV/00216224:14310/19:00112870 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.cell.com/biophysj/fulltext/S0006-3495(18)34025-6#articleInformation" target="_blank" >https://www.cell.com/biophysj/fulltext/S0006-3495(18)34025-6#articleInformation</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpj.2018.11.2760" target="_blank" >10.1016/j.bpj.2018.11.2760</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Kink in Helical Peptides Affects Membrane Pore Formation

Popis výsledku v původním jazyce

Antimicrobial peptides (AMPs) can kill pathogenic cells via the formation of membrane pores. However, the connection between peptide properties and their effect on pore formation remains elusive. In particular, the role of proline/glycine kink in helical AMPs has been reported with contradictory effects on antimicrobial activity. Using computer simulations and fluorescence leakage experiments we show the relationship between alpha-helical kink and the structure of the formed pore. Reconciling previous data, the presence of kinks was found to have both stabilizing or destabilizing effect, depending on the pore structure. Moreover, the position of proline/glycine kink in AMP sequence controls the peptide arrangements in the stabilized pores. The provided knowledge can be utilized to rationally design peptides with different ability to form membrane pores useful for the development of new antibacterial agents. To read this article in full you will need to make a payment

Název v anglickém jazyce

Kink in Helical Peptides Affects Membrane Pore Formation

Popis výsledku anglicky

Antimicrobial peptides (AMPs) can kill pathogenic cells via the formation of membrane pores. However, the connection between peptide properties and their effect on pore formation remains elusive. In particular, the role of proline/glycine kink in helical AMPs has been reported with contradictory effects on antimicrobial activity. Using computer simulations and fluorescence leakage experiments we show the relationship between alpha-helical kink and the structure of the formed pore. Reconciling previous data, the presence of kinks was found to have both stabilizing or destabilizing effect, depending on the pore structure. Moreover, the position of proline/glycine kink in AMP sequence controls the peptide arrangements in the stabilized pores. The provided knowledge can be utilized to rationally design peptides with different ability to form membrane pores useful for the development of new antibacterial agents. To read this article in full you will need to make a payment

Druh

O - Ostatní výsledky

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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