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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F12%3A43893975" target="_blank" >RIV/60461373:22330/12:43893975 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    D - Article in proceedings

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Article name in the collection

    Proceedings of 32nd European Peptide Symposium

  • ISBN

    978-960-466-121-3

  • ISSN

  • e-ISSN

  • Number of pages

    2

  • Pages from-to

    152-153

  • Publisher name

    JOHN WILEY & SONS INC

  • Place of publication

    HOBOKEN

  • Event location

    Athens

  • Event date

    Sep 2, 2012

  • Type of event by nationality

    EUR - Evropská akce

  • UT code for WoS article

    000308091500117