Modeling of the Antiviral Peptide for Specific Inhibition of Influenza Virus Entry

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F15%3A43907813" target="_blank" >RIV/62156489:43210/15:43907813 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.jscimedcentral.com/DrugDesign/drugdesign-2-1010.pdf" target="_blank" >http://www.jscimedcentral.com/DrugDesign/drugdesign-2-1010.pdf</a>

DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Modeling of the Antiviral Peptide for Specific Inhibition of Influenza Virus Entry

Popis výsledku v původním jazyce

Influenza is a highly pathogenic virus well known by a higher mutation rate, resulted from antigenic drift and shift of its surface proteins. The hemagglutinin- influenza major virus surface protein is responsible for viral entry through targeting sialicacid present on the lipid membrane of the host cell. Nowadays, peptides become the perspective therapeutic agents for various infection diseases including influenza. Utilization of peptides could provide high specifity, attained by a number of possiblemodifications, which can be simply proposed by using in silicomodeling. Molecular modeling of peptides with high affinity towards sialic acid binding site of influenza hemagglutinin may be thus helpful for inhibition of viral entry. Hence, we employed Yasara program for molecular modeling to estimate a binding energy of selected peptides to specific hemagglutinin binding site in the amino acids range of 116 - 261. We designed a mimicking peptide with sequence WLVFFVIFYIFR showing binding

Název v anglickém jazyce

Modeling of the Antiviral Peptide for Specific Inhibition of Influenza Virus Entry

Popis výsledku anglicky

Influenza is a highly pathogenic virus well known by a higher mutation rate, resulted from antigenic drift and shift of its surface proteins. The hemagglutinin- influenza major virus surface protein is responsible for viral entry through targeting sialicacid present on the lipid membrane of the host cell. Nowadays, peptides become the perspective therapeutic agents for various infection diseases including influenza. Utilization of peptides could provide high specifity, attained by a number of possiblemodifications, which can be simply proposed by using in silicomodeling. Molecular modeling of peptides with high affinity towards sialic acid binding site of influenza hemagglutinin may be thus helpful for inhibition of viral entry. Hence, we employed Yasara program for molecular modeling to estimate a binding energy of selected peptides to specific hemagglutinin binding site in the amino acids range of 116 - 261. We designed a mimicking peptide with sequence WLVFFVIFYIFR showing binding

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

<a href="/cs/project/GAP102%2F11%2F1068" target="_blank" >GAP102/11/1068: Nano-elektro-bio-nástroje pro biochemické a molekulárně-biologické studie eukaryotických buněk (NanoBioTECell)</a><br>

Návaznosti

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

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Journal of Drug Design and Research

ISSN

2379-089X

e-ISSN

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Svazek periodika

2

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

2

Strana od-do

"nestrankovano"

Kód UT WoS článku

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EID výsledku v databázi Scopus

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