Naslov
Molecular docking study of a novel series of pyrazolines as potential inhibitors of phosphodiesterase type 5 (PDE5)

Autori
Rastija, Vesna ; Molnar, Maja ; , Brahmbhatt, Harshad

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of Abstracts, 26th Croatian Meeting of Chemists and Chemical Engineers / Nives, Galić ; Marko, Rogošić - Zagreb : Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI), 2019, 152-152

ISBN
978953689467-3

Skup
26. hrvatski skup kemičara i kemijskih inženjera (26HSKIKI) ; 4. simpozij Vladimir Prelog

Mjesto i datum
Šibenik, Hrvatska, 09.04.2019. - 12.04.2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
pyrazolines ; phosphodiesterase ; molecular docking

Sažetak
Phosphodiesterase type 5 (PDE5) is a cyclic guanosine monophosphate (cGMP)-specific enzyme and mostly expressed in smooth muscle tissue of corpus cavernosum, heart, lung, platelets, prostate, urethra, bladder, liver, brain, and stomach. Inhibitors of PDE5, prevent the hydrolysis of cGMP and become effective treatment to diseases associated with low cGMP level, such as pulmonary arterial hypertension. [1] It has been well-documented that pyrazole- containing compounds diverse chemotherapeutic potentials, such as antileukemic and antiproliferative agents. Beside, halogenated organic compounds has been widely use as many drug candidates. [2] Recently, we have synthesized a novel series of halogenated pyrazolines. Molecular docking study was performed to explain in silico the binding interaction with the PDE5 (PDB: 4oew). Molecular docking has confirmed that compound 5-(2, 6-dimethoxyphenyl)-3-(4-fluorophenyl)-4, 5-dihydro-1H-pyrazole-1-carbaldehyde has lowest total energy binding (-105, 69 kcal/mol). The binding interactions of the most active compound have shown strong hydrogen bonding and van der Waals interactions with the target protein.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Farmacija

POVEZANOST RADA