Design, Synthesis, and Biological Effect Studies of Novel Benzofuran-Thiazolylhydrazone Derivatives as Monoamine Oxidase Inhibitors

Derya Osmani Ye; Begüm Nurpelin Sağlik; Serkan Levent; Ulviye Acar Çevi K; Sinem Ilgin; Leyla Yurttaş; Yusuf Özkay; Ahmet Cagri Karaburun; Zafer Asım Kaplancikli; Nalan Gundogdu-Karaburun

doi:10.1021/acsomega.3c07703

Design, Synthesis, and Biological Effect Studies of Novel Benzofuran-Thiazolylhydrazone Derivatives as Monoamine Oxidase Inhibitors

ACS Omega. 2024 Feb 29;9(10):11388-11397. doi: 10.1021/acsomega.3c07703. eCollection 2024 Mar 12.

Authors

Derya Osmani Ye^{1

2}, Begüm Nurpelin Sağlik^{1

2}, Serkan Levent^{1

2}, Ulviye Acar Çevi K^{1

2}, Sinem Ilgin³, Leyla Yurttaş¹, Yusuf Özkay^{1

2}, Ahmet Cagri Karaburun¹, Zafer Asım Kaplancikli¹, Nalan Gundogdu-Karaburun¹

Affiliations

¹ Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Anadolu University, 26470 Eskişehir, Turkey.
² Central Research Laboratory (MERLAB), Faculty of Pharmacy, Anadolu University, 26470 Eskişehir, Turkey.
³ Department of Pharmaceutical Toxicology, Faculty of Pharmacy, Anadolu University, 26470 Eskişehir, Turkey.

Abstract

In recent studies, monoamine oxidase (MAO) inhibitory effects of various thiazolylhydrazone derivatives have been demonstrated. Within the scope of this study, 12 new compounds containing thiazolylhydrazone groups were synthesized. The structures of the obtained compounds were elucidated by ¹H NMR, ¹³C NMR, and high-resolution mass spectrometry (HRMS) methods. The inhibitory effects of the final compounds on MAO enzymes were investigated by means of in vitro methods. In addition to enzyme inhibition studies, enzyme kinetic studies of compounds with high inhibitory activity were examined, and their effects on substrate-enzyme relations were investigated. Additionaly, cytotoxicity tests were carried out to determine the toxicities of the selected compounds, and the compounds were found to be nontoxic. The interactions of the active compound with the active site of the enzyme were characterized by in silico methods.