Dynamics of lipid layers with/without bounded antimicrobial peptide halictine-1

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00484564" target="_blank" >RIV/61388963:_____/17:00484564 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11320/17:10366928

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.vibspec.2017.10.002" target="_blank" >http://dx.doi.org/10.1016/j.vibspec.2017.10.002</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.vibspec.2017.10.002" target="_blank" >10.1016/j.vibspec.2017.10.002</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Dynamics of lipid layers with/without bounded antimicrobial peptide halictine-1

Popis výsledku v původním jazyce

Dynamic behavior during the drying process of phospholipid multilayers composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine and 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-rac-glycerol) in mixtures of 1:4, was investigated by means of attenuated total reflection (ATR) Fourier transform infrared spectroscopy (FTIR). The interaction of the antimicrobial peptide halictine-1 (HAL-1), a linear dodecapeptide isolated from the venom of eusocial bee Halictus sexcinctus, with the lipid layer and its influence on the dynamics of the lipid layer was also studied. Analysis of ATR-FTIR spectra of the drying process by principal component analysis (PCA) clearly showed the sensitivity of C=O vibrations at 1737 cm(-1), PO2 vibrations in the region 1000-1250 cm(-1) and CH stretching vibrations at 2850 and 2950 cm-1 to the hydration of the lipid layer. Nevertheless, PCA revealed that the lipid layers periodically oscillate between dehydration/hydration states. The protective influence of HAL-1 on the lipid layer, including the disappearance of dehydration/hydration oscillations, and slowing down of the drying of the system in the presence of the peptide was observed. PCA indicates a two-stage process of the interaction of HAL-1 with lipid layers and as well as the influence of HAL-1 on vibrations of the C=O and PO2 of lipid groups, whereas CH2 and CH3 vibrations remain intact during the binding of the peptide. The peptide binds to phospholipid head groups, changes its structure from a random coil to an alpha-helix structure, and interacts with the C=O groups of the lipids, staying on the surface of the membrane.

Název v anglickém jazyce

Dynamics of lipid layers with/without bounded antimicrobial peptide halictine-1

Popis výsledku anglicky

Dynamic behavior during the drying process of phospholipid multilayers composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine and 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-rac-glycerol) in mixtures of 1:4, was investigated by means of attenuated total reflection (ATR) Fourier transform infrared spectroscopy (FTIR). The interaction of the antimicrobial peptide halictine-1 (HAL-1), a linear dodecapeptide isolated from the venom of eusocial bee Halictus sexcinctus, with the lipid layer and its influence on the dynamics of the lipid layer was also studied. Analysis of ATR-FTIR spectra of the drying process by principal component analysis (PCA) clearly showed the sensitivity of C=O vibrations at 1737 cm(-1), PO2 vibrations in the region 1000-1250 cm(-1) and CH stretching vibrations at 2850 and 2950 cm-1 to the hydration of the lipid layer. Nevertheless, PCA revealed that the lipid layers periodically oscillate between dehydration/hydration states. The protective influence of HAL-1 on the lipid layer, including the disappearance of dehydration/hydration oscillations, and slowing down of the drying of the system in the presence of the peptide was observed. PCA indicates a two-stage process of the interaction of HAL-1 with lipid layers and as well as the influence of HAL-1 on vibrations of the C=O and PO2 of lipid groups, whereas CH2 and CH3 vibrations remain intact during the binding of the peptide. The peptide binds to phospholipid head groups, changes its structure from a random coil to an alpha-helix structure, and interacts with the C=O groups of the lipids, staying on the surface of the membrane.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/GAP208%2F10%2F0376" target="_blank" >GAP208/10/0376: Modelování interakce antibakteriálních peptidů s modelovou membránou a možnost predikce jejich biologické aktivity</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Vibrational Spectroscopy

ISSN

0924-2031

e-ISSN

—

Svazek periodika

93

Číslo periodika v rámci svazku

Nov

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

10

Strana od-do

42-51

Kód UT WoS článku

000418986800007

EID výsledku v databázi Scopus

2-s2.0-85032856507