Inactivation of human dipeptidyl peptidase III by quinazolinone derivatives (CROSBI ID 702696)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Agić, Dejan ; Karnaš, Maja ; Šubarić, Domagoj ; Komar, Mario ; Karačić, Zrinka ; Tomić, Sanja ; Molnar, Maja
engleski
Inactivation of human dipeptidyl peptidase III by quinazolinone derivatives
Human dipeptidyl peptidase III (hDPP III) is a zinc‐hydrolase that cleaves dipeptides from the N‐ terminal of different bioactive peptides. Quinazolinones belong to a diverse class of nitrogen-containing heterocyclic compounds, derivatives of which exhibit a wide range of biological activities. In this research, we selected 10 previously synthesized [1] structuraly different quinazolinone derivatives (QDs) to investigate their potential to inactivate hDPP III activity combining in vitro and in silico approach. The experimental results showed that all analyzed QDs (at the physiological concentration i.e., 100 μM) have inhibitory effect against hDPP III activity. The strongest inhibition (% inh. = 81.9) has been obtained with compound QD8. Molecular docking revealed that hDPP III interacts mostly by hydrogen bonds and hydrophobic interactions with QD8. Among important intermolecular interactions are those with amino acid residues F443, Q446, V447, H568 and R572 that are constituents of hDPP III substrate binding subsites S1, S1’, S2’, and S3’.
dipeptidyl peptidase III ; quinazolinones ; molecular docking
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
Podaci o prilogu
124-124.
2020.
objavljeno
Podaci o matičnoj publikaciji
Book of abstracts - 18th Ružička days
Jukić, Ante
Zagreb : Osijek: Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI)
978-953-6894-75-8
Podaci o skupu
18. Ružičkini dani "Danas znanost - sutra industrija"
poster
16.09.2020-18.09.2020
Vukovar, Hrvatska