Vibrational circular dichroism study of polypeptide model-membrane systems

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F12%3A43893351" target="_blank" >RIV/60461373:22340/12:43893351 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.ab.2012.03.023" target="_blank" >http://dx.doi.org/10.1016/j.ab.2012.03.023</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ab.2012.03.023" target="_blank" >10.1016/j.ab.2012.03.023</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Vibrational circular dichroism study of polypeptide model-membrane systems

Popis výsledku v původním jazyce

In this article, we describe the mutual structural effect of the interaction between the model membranes and polylysine and poly-L-arginine. Vibrational circular dichroism (VCD), a method exceptionally sensitive to the polypeptide structure that has notbeen established in such studies before, was the primary method of this study. A complementary technique, electronic circular dichroism, was applied to verify the newly obtained results and as a bridge to the previous studies. We used micelles composed of sodium dodecyl sulfate (SDS) as a monolayer membrane model and large unilamellar vesicles composed of phospholipids as a bilayer membrane model. We describe the conformational changes of the polypeptides caused by the interaction with the model membranes. Among others, the presence of the liposomes in the solution generated special conditions for the formation of the alpha-helical structure of poly-L-arginine; the presence of SDS induced the formation of the beta-structure of polylysin

Název v anglickém jazyce

Vibrational circular dichroism study of polypeptide model-membrane systems

Popis výsledku anglicky

In this article, we describe the mutual structural effect of the interaction between the model membranes and polylysine and poly-L-arginine. Vibrational circular dichroism (VCD), a method exceptionally sensitive to the polypeptide structure that has notbeen established in such studies before, was the primary method of this study. A complementary technique, electronic circular dichroism, was applied to verify the newly obtained results and as a bridge to the previous studies. We used micelles composed of sodium dodecyl sulfate (SDS) as a monolayer membrane model and large unilamellar vesicles composed of phospholipids as a bilayer membrane model. We describe the conformational changes of the polypeptides caused by the interaction with the model membranes. Among others, the presence of the liposomes in the solution generated special conditions for the formation of the alpha-helical structure of poly-L-arginine; the presence of SDS induced the formation of the beta-structure of polylysin

Druh

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

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

—

Návaznosti

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 periodika

Analytical Biochemistry

ISSN

0003-2697

e-ISSN

—

Svazek periodika

427

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

211-218

Kód UT WoS článku

000306872200019

EID výsledku v databázi Scopus

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