Synthesis of a Fluorescent Probe for Sensing Multiple Protein States

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00495680" target="_blank" >RIV/61388963:_____/18:00495680 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/ejoc.201800524" target="_blank" >http://dx.doi.org/10.1002/ejoc.201800524</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/ejoc.201800524" target="_blank" >10.1002/ejoc.201800524</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Synthesis of a Fluorescent Probe for Sensing Multiple Protein States

Popis výsledku v původním jazyce

We synthesized solvatochromic thiol-reactive fluorescent probes 6FM-M and 7AFM-M possessing two-band emission. 7AFM-M was designed to have a smaller dipole moment than 6FM-M and as a result it showed better separation of the two emission bands. Both probes were used to label a cysteine mutant of α-synuclein (αSyn), a presynaptic neuronal protein associated with Parkinson's disease. We investigated the ability of the probes to sense αSyn binding to lipid membranes and αSyn fibrillization, and compared their sensitivity with that of one-band solvatochromic probes. We found that while all the tested probes can discriminate two αSyn states, only the 7AFM-M probe is able to clearly discriminate all three protein states of αSyn: unstructured, membrane-bound and fibrillar αSyn. Finally, using αSyn labelled with 7AFM-M, we demonstrated that high density of αSyn on lipid membranes may lead to the partial membrane destruction with a formation of lipoprotein particles.

Název v anglickém jazyce

Synthesis of a Fluorescent Probe for Sensing Multiple Protein States

Popis výsledku anglicky

We synthesized solvatochromic thiol-reactive fluorescent probes 6FM-M and 7AFM-M possessing two-band emission. 7AFM-M was designed to have a smaller dipole moment than 6FM-M and as a result it showed better separation of the two emission bands. Both probes were used to label a cysteine mutant of α-synuclein (αSyn), a presynaptic neuronal protein associated with Parkinson's disease. We investigated the ability of the probes to sense αSyn binding to lipid membranes and αSyn fibrillization, and compared their sensitivity with that of one-band solvatochromic probes. We found that while all the tested probes can discriminate two αSyn states, only the 7AFM-M probe is able to clearly discriminate all three protein states of αSyn: unstructured, membrane-bound and fibrillar αSyn. Finally, using αSyn labelled with 7AFM-M, we demonstrated that high density of αSyn on lipid membranes may lead to the partial membrane destruction with a formation of lipoprotein particles.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10401 - Organic chemistry

Projekt

<a href="/cs/project/GJ18-06255Y" target="_blank" >GJ18-06255Y: Nová strategie pro inhibici tvorby amyloidních fibril</a><br>

Návaznosti

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

European Journal of Organic Chemistry

ISSN

1434-193X

e-ISSN

—

Svazek periodika

2018

Číslo periodika v rámci svazku

37

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

8

Strana od-do

5155-5162

Kód UT WoS článku

000446662900010

EID výsledku v databázi Scopus

2-s2.0-85052462248