Fluorescent Probe for Selective Imaging of a-Synuclein Fibrils in Living Cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F21%3A10430070" target="_blank" >RIV/00216208:11310/21:10430070 - isvavai.cz</a>

Výsledek na webu

<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=VTzwtQjy_4" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=VTzwtQjy_4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acschemneuro.1c00090" target="_blank" >10.1021/acschemneuro.1c00090</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Fluorescent Probe for Selective Imaging of a-Synuclein Fibrils in Living Cells

Popis výsledku v původním jazyce

Plaques of amyloid fibrils composed of neuronal protein alpha-synuclein are one of the hallmarks of Parkinson&apos;s disease, and their selective imaging is crucial to study the mechanism of its pathogenesis. However, the existing fluorescent probes for amyloids are efficient only in solution and tissue systems, and they are not selective enough for the visualization of amyloid fibrils in living cells. In this study, we present two molecular rotor-based probes RB1 and RB2. These thiazolium probes show affinity to alpha-synuclein fibrils and turn-on fluorescence response upon interactions. Because of its extended pi-conjugation and high rotational degree of freedom, RB1 exhibits a 76 nm red-shift of absorption maxima and 112-fold fluorescence enhancement upon binding to amyloid fibrils. Owing to its strong binding affinity to alpha-synuclein fibrils, RB1 can selectively stain them in the cytoplasm of living HeLa and SH-SY5Y cells with high optical contrast. RB1 is a cell-permeable and noncytotoxic probe. Taken together, we have demonstrated that RB1 is an amyloid probe with an outstanding absorption red-shift that can be used for intracellular imaging of alpha-synuclein fibrils.

Název v anglickém jazyce

Fluorescent Probe for Selective Imaging of a-Synuclein Fibrils in Living Cells

Popis výsledku anglicky

Plaques of amyloid fibrils composed of neuronal protein alpha-synuclein are one of the hallmarks of Parkinson&apos;s disease, and their selective imaging is crucial to study the mechanism of its pathogenesis. However, the existing fluorescent probes for amyloids are efficient only in solution and tissue systems, and they are not selective enough for the visualization of amyloid fibrils in living cells. In this study, we present two molecular rotor-based probes RB1 and RB2. These thiazolium probes show affinity to alpha-synuclein fibrils and turn-on fluorescence response upon interactions. Because of its extended pi-conjugation and high rotational degree of freedom, RB1 exhibits a 76 nm red-shift of absorption maxima and 112-fold fluorescence enhancement upon binding to amyloid fibrils. Owing to its strong binding affinity to alpha-synuclein fibrils, RB1 can selectively stain them in the cytoplasm of living HeLa and SH-SY5Y cells with high optical contrast. RB1 is a cell-permeable and noncytotoxic probe. Taken together, we have demonstrated that RB1 is an amyloid probe with an outstanding absorption red-shift that can be used for intracellular imaging of alpha-synuclein fibrils.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

ACS Chemical Neuroscience

ISSN

1948-7193

e-ISSN

—

Svazek periodika

12

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

1293-1298

Kód UT WoS článku

000643598600002

EID výsledku v databázi Scopus

2-s2.0-85104917599