Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F16%3A43901665" target="_blank" >RIV/60461373:22340/16:43901665 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/16:00463448
Result on the web
<a href="http://dx.doi.org/10.1007/s00706-016-1807-6" target="_blank" >http://dx.doi.org/10.1007/s00706-016-1807-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00706-016-1807-6" target="_blank" >10.1007/s00706-016-1807-6</a>

Result language
angličtina
Original language name
Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides
Original language description
Antimicrobial and hemolytic activities of cationic alpha-helical antimicrobial peptides depend on their ability to adopt an amphipathic alpha-helical conformation on the cell membrane surface. Using vibrational and electronic circular dichroism, we carried out a conformational study of two alpha-helical antimicrobial peptides, melectin and antapin, in various environments mimicking bacterial and eukaryotic membranes. The results showed a significant difference in the content of alpha-helical conformation in the environment mimicking the bacterial and eukaryotic membranes.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
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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)

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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