Fine tuning of cholinesterase and glutathione-S-transferase activities by organoruthenium(II) complexes

Trobec, Tomaž (avtor), Sepčić, Kristina (avtor), Žužek, Monika C. (avtor), Kladnik, Jerneja (avtor), Podjed, Nina (avtor), Cardoso Páscoa, Catarina (avtor), Turel, Iztok (avtor), Frangež, Robert (avtor)

Cholinesterases (ChEs) show increased activities in patients with Alzheimer’s disease, and remain one of the main therapeutic targets for treatment of this neurodegenerative disorder. A library of organoruthenium(II) complexes was prepared to investigate the influence of their structural elements on inhibition of ChEs, and on another pharmacologically important group of enzymes, glutathione S-transferases (GSTs). Two groups of organoruthenium(II) compounds were considered: (i) organoruthenium(II) complexes with p-cymene as an arene ligand, and (ii) organoruthenium(II) carbonyl complexes as CO-releasing molecules. Eight organoruthenium complexes were screened for inhibitory activities against ChEs and GSTs of human and animal origins. Some compounds inhibited all of these enzymes at low micromolar concentrations, while others selectively inhibited either ChEs or GSTs. This study demonstrates the importance of the different structural elements of organoruthenium complexes for their inhibitory activities against ChEs and GSTs, and also proposes some interesting compounds for further preclinical testing as ChE or GST inhibitory drugs.

• Jezik: Angleški jezik
• Ključne besede: cholinesterase, enzyme inhibition, glutathione S-transferase, organoruthenium complex, pyrithione, β-diketone, carbonyl, glutathione transferase
• Vrsta gradiva: Članek v reviji
• Tipologija: 1.01 - Izvirni znanstveni članek
• Organizacija: VF - Veterinarska fakulteta ; BF - Biotehniška fakulteta ; FKKT - Fakulteta za kemijo in kemijsko tehnologijo
• Status publikacije: Objavljeno
• Različica publikacije: Objavljena publikacija
• Leto izida: 2021
• Št. strani: 16 str.
• Številčenje: Vol. 9, iss. 9, art. 1243
• PID: 20.500.12556/RUL-136344
• UDK: 636.09:612
• ISSN pri članku: 2227-9059
• DOI: 10.3390/biomedicines9091243
• COBISS.SI-ID: 76757507
• Datum objave v RUL: 25.04.2022

Gradivo je del revije

• Naslov: Biomedicines
• Skrajšan naslov: Biomedicines
• Založnik: MDPI AG
• ISSN: 2227-9059
• COBISS.SI-ID: 523006745

Licence

• Licenca: CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
• Povezava: http://creativecommons.org/licenses/by/4.0/deed.sl
• Opis: To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
• Začetek licenciranja: 16.09.2021