The Red Shift in Estrogen Research An Estrogen-Receptor Targeted aza-BODIPY–Estradiol Fluorescent Conjugate /

Estradiol (E2) plays an important role in cell proliferation and certain brain functions. To reveal its mechanism of action, its detectability is essential. Only a few fluorescent-labeled hormonally active E2s exist in the literature, and their mechanism of action usually remains unclear. It would b...

Teljes leírás

Elmentve itt :
Bibliográfiai részletek
Szerzők: Hlogyik Tamás
Bózsity-Faragó Noémi
Börzsei Rita
Kovács Benjamin
Labos Péter
Hetényi Csaba
Csontné Kiricsi Mónika
Huliák Ildikó
Kele Zoltán
Poór Miklós
Erostyák János
Hunyadi Attila
Zupkó István
Mernyák Erzsébet
Dokumentumtípus: Cikk
Megjelent: 2025
Sorozat:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 26 No. 15
Tárgyszavak:
doi:10.3390/ijms26157075

mtmt:36263554
Online Access:http://publicatio.bibl.u-szeged.hu/37607
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245 1 4 |a The Red Shift in Estrogen Research  |h [elektronikus dokumentum] :  |b An Estrogen-Receptor Targeted aza-BODIPY–Estradiol Fluorescent Conjugate /  |c  Hlogyik Tamás 
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520 3 |a Estradiol (E2) plays an important role in cell proliferation and certain brain functions. To reveal its mechanism of action, its detectability is essential. Only a few fluorescent-labeled hormonally active E2s exist in the literature, and their mechanism of action usually remains unclear. It would be of particular interest to develop novel labeled estradiol derivatives with retained biological activity and improved optical properties. Due to their superior optical characteristics, aza-BODIPY dyes are frequently used labeling agents in biomedical applications. E2 was labeled with the aza-BODIPY dye at its phenolic hydroxy function via an alkyl linker and a triazole coupling moiety. The estrogenic activity of the newly synthesized fluorescent conjugate was evaluated via transcriptional luciferase assay. Docking calculations were performed for the classical and alternative binding sites (CBS and ABS) of human estrogen receptor α. The terminal alkyne function was introduced into the tetraphenyl aza-BODIPY core via selective formylation, oxidation, and subsequent amidation with propargyl amine. The conjugation was achieved via Cu(I)-catalyzed azide–alkyne click reaction of the aza-BODIPY-alkyne with the 3-O-(4-azidobut-1-yl) derivative of E2. The labeled estrogen induced a dose-dependent transcriptional activity of human estrogen receptor α with a submicromolar EC50 value. Docking calculations revealed that the steroid part has a perfect overlap with E2 in ABS. In CBS, however, a head-tail binding deviation was observed. A facile, fluorescent labeling methodology has been elaborated for the development of a novel red-emitting E2 conjugate with substantial estrogenic activity. Docking experiments uncovered the binding mode of the conjugate in both ABS and CBS. 
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700 0 2 |a Bózsity-Faragó Noémi  |e aut 
700 0 2 |a Börzsei Rita  |e aut 
700 0 2 |a Kovács Benjamin  |e aut 
700 0 2 |a Labos Péter  |e aut 
700 0 2 |a Hetényi Csaba  |e aut 
700 0 2 |a Csontné Kiricsi Mónika  |e aut 
700 0 2 |a Huliák Ildikó  |e aut 
700 0 2 |a Kele Zoltán  |e aut 
700 0 2 |a Poór Miklós  |e aut 
700 0 2 |a Erostyák János  |e aut 
700 0 2 |a Hunyadi Attila  |e aut 
700 0 2 |a Zupkó István  |e aut 
700 0 2 |a Mernyák Erzsébet  |e aut 
856 4 0 |u http://publicatio.bibl.u-szeged.hu/37607/1/ijms-26-07075.pdf  |z Dokumentum-elérés