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Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475296" target="_blank" >RIV/61388963:_____/17:00475296 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22320/17:43913252 RIV/60461373:22340/17:43913252

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.saa.2016.07.015" target="_blank" >http://dx.doi.org/10.1016/j.saa.2016.07.015</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.saa.2016.07.015" target="_blank" >10.1016/j.saa.2016.07.015</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

  • Original language description

    Antimicrobial peptides have long been considered as promising compounds against drug-resistant pathogens. In this work, we studied the secondary structure of antimicrobial peptides melectin and antapin using electronic (ECD) and vibrational circular dichroism (VCD) spectroscopies that are sensitive to peptide secondary structures. The results from quantitative ECD spectral evaluation by Dichroweb and CDNN program and from the qualitative evaluation of the VCD spectra were compared. The antimicrobial activity of the selected peptides depends on their ability to adopt an amphipathic alpha-helical conformation on the surface of the bacterial membrane. Hence, solutions of different zwitterionic and negatively charged liposomes and micelles were used to mimic the eukaryotic and bacterial biological membranes. The results show a significant content of alpha-helical conformation in the solutions of negatively charged liposomes mimicking the bacterial membrane, thus correlating with the antimicrobial activity of the studied peptides. On the other hand in the solutions of zwitterionic liposomes used as models of the eukaryotic membranes, the fraction of alpha-helical conformation was lower, which corresponds with their moderate hemolytic activity.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10406 - Analytical chemistry

Result continuities

  • Project

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

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

  • ISSN

    1386-1425

  • e-ISSN

  • Volume of the periodical

    170

  • Issue of the periodical within the volume

    Jan 5

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    247-255

  • UT code for WoS article

    000398746600033

  • EID of the result in the Scopus database

    2-s2.0-84978405312