A new series of naphthyl-thiosemicarbazone and thio/carbohydrazone derivatives: Synthesis, spectroscopic elucidation, dual enzyme inhibition targeting carbonic anhydrase/ acetylcholinesterase and molecular docking studies

Yakan, Hasan; MUĞLU, Halit; Erdoğan, Musa; Türkeş, Cüneyt; Demir, Yeliz

doi:10.1016/j.abb.2025.110491

A new series of naphthyl-thiosemicarbazone and thio/carbohydrazone derivatives: Synthesis, spectroscopic elucidation, dual enzyme inhibition targeting carbonic anhydrase/ acetylcholinesterase and molecular docking studies

Yazarlar (5)
Hasan Yakan Ondokuz Mayis Üniversitesi, Turkey
Doç. Dr. Halit MUĞLU Kurum Bilgileri Fen Fakültesi Kimya Kimya Özgeçmiş Sayfası İletişim Bilgileri: (366)280-1000 kastamonu Üniversitesi fen edebiyat fakültesi kimya bölümü Merkez/kastamonu Kastamonu Üniversitesi, Türkiye
Musa Erdoğan Kafkas Üniversitesi, Turkey
Cüneyt Türkeş Erzincan Binali Yıldırım Üniversitesi, Turkey
Yeliz Demir Ardahan Üniversitesi, Turkey

Devamını Göster

Özet

New naphthyl-thiosemicarbazone derivatives (1–9) were obtained from 1-naphthaldehyde and numerous thiosemicarbazides. New naphthyl-thio/carbohydrazones (10–12) were prepared from 1-naphthaldehyde and various thio/carbohydrazides. FT-IR, ¹H NMR, ¹³C NMR, and elemental analysis were used to elucidate the structures of the newly obtained compounds. The inhibitory effects of these compounds against human carbonic anhydrase isoforms I and II (hCA I and hCA II) and acetylcholinesterase (AChE) were systematically evaluated. Several compounds exhibited potent inhibition, particularly derivatives bearing halogenated and electron-donating aromatic substituents. Among them, compound 11 demonstrated the strongest inhibition for all three enzymes, with KI values of 52.42 nM (hCA I), 59.23 nM (hCA II), and 40.16 nM (AChE), surpassing the reference standards acetazolamide and tacrine. Structure–activity relationship (SAR) analysis highlighted the critical influence of substituent type and position on enzymatic activity. In addition, molecular docking simulations were conducted to elucidate the binding interactions of the most potent compound with hCA I, hCA II, and AChE enzymes. The docking results supported the in vitro findings, revealing favorable binding energies and key interactions such as π–π stacking and hydrogen bonding, especially for compound 11.

Anahtar Kelimeler

Makale Türü	Özgün Makale
Makale Alt Türü	SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale
Dergi Adı	Archives of Biochemistry and Biophysics
Dergi ISSN	0003-9861 Wos Dergi Scopus Dergi
Dergi Grubu	Q1
Makale Dili	İngilizce
Basım Tarihi	09-2025
Cilt No	771
Sayı	1
Doi Numarası	10.1016/j.abb.2025.110491

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Atıf Sayıları

A new series of naphthyl-thiosemicarbazone and thio/carbohydrazone derivatives: Synthesis, spectroscopic elucidation, dual enzyme inhibition targeting carbonic anhydrase/ acetylcholinesterase and molecular docking studies

Akademisyenler > Halit MUĞLU > Yayın Detayı

A new series of naphthyl-thiosemicarbazone and thio/carbohydrazone derivatives: Synthesis, spectroscopic elucidation, dual enzyme inhibition targeting carbonic anhydrase/ acetylcholinesterase and molecular docking studies

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