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)

Doç. Dr. Hasan Yakan Ondokuz Mayis Üniversitesi, Türkiye

Prof. Dr. Halit MUĞLU Kastamonu Üniversitesi, Türkiye

Musa Erdoğan Kafkas Üniversitesi, Türkiye

Prof. Dr. Cüneyt Türkeş Erzincan Binali Yıldırım Üniversitesi, Türkiye

Prof. Dr. Yeliz Demir Ardahan Üniversitesi, Türkiye

Makale Türü	Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı	Archives of Biochemistry and Biophysics (Q2)
Dergi ISSN	0003-9861 Wos Dergi Scopus Dergi
Dergi Tarandığı Indeksler	SCI-Expanded
Makale Dili	İngilizce	Basım Tarihi	10-2025
Cilt / Sayı / Sayfa	771 / 1 / –	DOI	10.1016/j.abb.2025.110491
Makale Linki	https://doi.org/10.1016/j.abb.2025.110491

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

Science Direct

BM Sürdürülebilir Kalkınma Amaçları

Atıf Sayıları
Scopus	4

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

Dergi Adı	ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Yayıncı	Academic Press Inc.
Açık Erişim	Hayır
ISSN	0003-9861
E-ISSN	1096-0384
CiteScore	6,4
SJR	0,912
SNIP	0,784

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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