Effect of melittin on influenza-infected chicken embryos

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F15%3A43906905" target="_blank" >RIV/62156489:43210/15:43906905 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216305:26620/15:PU125884

Výsledek na webu

<a href="https://mnet.mendelu.cz/mendelnet2015/mnet_2015_full.pdf" target="_blank" >https://mnet.mendelu.cz/mendelnet2015/mnet_2015_full.pdf</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Effect of melittin on influenza-infected chicken embryos

Popis výsledku v původním jazyce

Antimicrobial peptides are peptides isolated from a wide range of organisms that exert microbicidal activity against a wide spectrum of targets, including bacteria, viruses, fungi, and parasites. These peptides are aimed directly on the phospholipid bilayer and do not target on the cellular or metabolic activities of the cells as antibiotics and other drugs do. But thanks to many vital proteins associated with the membrane, these peptides can also influence these structures and therefore facilitate andaccelerate their death. Melittin is a well-characterized pore-forming lytic amphiphilic peptide (consisting of 26 amino acids) found in bee venom. The amphiphilic property of this peptide makes it water-soluble and yet it spontaneously associates with natural and artificial membranes. This integration leads to the distortion and permeabilization of the membrane. In this study melittin has been utilized to study antiviral properties against influenza A virus. Melittin was used in the mixt

Název v anglickém jazyce

Effect of melittin on influenza-infected chicken embryos

Popis výsledku anglicky

Antimicrobial peptides are peptides isolated from a wide range of organisms that exert microbicidal activity against a wide spectrum of targets, including bacteria, viruses, fungi, and parasites. These peptides are aimed directly on the phospholipid bilayer and do not target on the cellular or metabolic activities of the cells as antibiotics and other drugs do. But thanks to many vital proteins associated with the membrane, these peptides can also influence these structures and therefore facilitate andaccelerate their death. Melittin is a well-characterized pore-forming lytic amphiphilic peptide (consisting of 26 amino acids) found in bee venom. The amphiphilic property of this peptide makes it water-soluble and yet it spontaneously associates with natural and artificial membranes. This integration leads to the distortion and permeabilization of the membrane. In this study melittin has been utilized to study antiviral properties against influenza A virus. Melittin was used in the mixt

Druh

D - Stať ve sborníku

CEP obor

GJ - Choroby a škůdci zvířat, veterinární medicina

OECD FORD obor

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Projekt

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Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název statě ve sborníku

MendelNet 2015: Proceedings of International PhD Students Conference

ISBN

978-80-7509-363-9

ISSN

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e-ISSN

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Počet stran výsledku

5

Strana od-do

475-479

Název nakladatele

Mendelova univerzita v Brně

Místo vydání

Brno

Místo konání akce

Brno

Datum konání akce

11. 11. 2015

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

000366466100090