De novo design of short peptides with antimicrobial activity and the effect of acyl conjugation

Kód výsledku v IS VaVaI

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Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

De novo design of short peptides with antimicrobial activity and the effect of acyl conjugation

Popis výsledku v původním jazyce

The alarming increase in number of resistant pathogenic microorganisms is the reason for the intense search for new antimicrobial agents. The short peptides belong among the newly discovered antimicrobial compounds. These peptides provide a large potential for fight against adaptable pathogens, but in few aspects, like production costs, longer peptides are disadvantageous compared to antibiotics. As potential therapeutic agents, short peptides with simple amino acid composition can be better candidates.We designed three peptides composed of six kinds of amino acids selected on the basis of statistical data from databases to gain amphipathic character and positive charge of peptides. The sequence of amino acids was arranged by three different ways, onewas based on relative frequency of occurrence of residues, to form helical conformation and all of these peptides were modified by C-terminal amidation. To investigate the importance of increased hydrophobicity at the amino end of peptid

Název v anglickém jazyce

De novo design of short peptides with antimicrobial activity and the effect of acyl conjugation

Popis výsledku anglicky

The alarming increase in number of resistant pathogenic microorganisms is the reason for the intense search for new antimicrobial agents. The short peptides belong among the newly discovered antimicrobial compounds. These peptides provide a large potential for fight against adaptable pathogens, but in few aspects, like production costs, longer peptides are disadvantageous compared to antibiotics. As potential therapeutic agents, short peptides with simple amino acid composition can be better candidates.We designed three peptides composed of six kinds of amino acids selected on the basis of statistical data from databases to gain amphipathic character and positive charge of peptides. The sequence of amino acids was arranged by three different ways, onewas based on relative frequency of occurrence of residues, to form helical conformation and all of these peptides were modified by C-terminal amidation. To investigate the importance of increased hydrophobicity at the amino end of peptid

Druh

D - Stať ve sborníku

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název statě ve sborníku

Proceedings of 32nd European Peptide Symposium

ISBN

978-960-466-121-3

ISSN

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e-ISSN

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Počet stran výsledku

2

Strana od-do

152-153

Název nakladatele

JOHN WILEY & SONS INC

Místo vydání

HOBOKEN

Místo konání akce

Athens

Datum konání akce

2. 9. 2012

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

000308091500117