Naslov
Inaktivacija ljudske dipeptidil peptidaze III derivatima kinazolinona
(Inactivation of human dipeptidyl peptidase III by quinazolinone derivatives)

Autori
Agić, Dejan ; Karnaš, Maja ; Šubarić, Domagoj ; Komar, Mario ; Karačić, Zrinka ; Tomić, Sanja ; Molnar, Maja

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

Izvornik
Book of abstracts - 18th Ružička days / Jukić, Ante - Zagreb : Osijek : Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI), 2020, 124-124

ISBN
978-953-6894-75-8

Skup
18. Ružičkini dani "Danas znanost - sutra industrija"

Mjesto i datum
Vukovar, Hrvatska, 16.09.2020. - 18.09.2020

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
dipeptidyl peptidase III ; quinazolinones ; molecular docking

Sažetak
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’.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Interdisciplinarne prirodne znanosti

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