Determination of biological studies and molecular docking calculations of isatin-thiosemicarbazone hybrid compounds

Koçyiğit, Ümit M.; Doğan, Murat; MUĞLU, Halit; Taslimi, Parham; Tüzün, Burak; Yakan, Hasan; Bal, Halil; Güzel, Emre; Gülçin, İlham

doi:10.1016/j.molstruc.2022.133249

Determination of biological studies and molecular docking calculations of isatin-thiosemicarbazone hybrid compounds

Yazarlar (9)

Ümit M. Koçyiğit
Cumhuriyet Üniversitesi, Türkiye

Doç. Dr. Murat Doğan Cumhuriyet Üniversitesi, Türkiye

Prof. Dr. Halit MUĞLU Kastamonu Üniversitesi, Türkiye

Doç. Dr. Parham Taslimi Bartin Üniversitesi, Türkiye

Burak Tüzün Cumhuriyet Üniversitesi, Türkiye

Doç. Dr. Hasan Yakan Ondokuz Mayis Üniversitesi, Türkiye

Dr. Öğr. Üyesi Halil Bal Cumhuriyet Üniversitesi, Türkiye

Prof. Dr. Emre Güzel Sakarya University Of Applied Sciences, Türkiye

İlham Gülçin
Atatürk Üniversitesi, Türkiye

Makale Türü	Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
Dergi Adı	Journal of Molecular Structure (Q2)
Dergi ISSN	0022-2860 Dergi Bilgileri (2022)
Dergi Tarandığı Indeksler	SCI-Expanded
Makale Dili	İngilizce	Basım Tarihi	09-2022
Kabul Tarihi	–	Yayınlanma Tarihi	01-09-2022
Cilt / Sayı / Sayfa	1264 / 1 / 133249–0	DOI	10.1016/j.molstruc.2022.133249
Makale Linki	http://dx.doi.org/10.1016/j.molstruc.2022.133249
UAK Araştırma Alanları	Organik Kimya Spektroskopi Biyokimya

Özet

Design, synthesis, structural elucidation, and investigation of cytotoxic and antimicrobial activity, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE) enzyme inhibition effects of isatin-thiosemicarbazone hybrid compounds (1–15) are reported in this study. Hybrid compounds (14 and 15) were synthesized, isolated, and characterized for the first time. FT-IR, ¹H NMR, and ¹³C NMR spectroscopic methods and elemental analysis were used to characterize the structures of the compounds. In the enzymatic evaluation, hybrid compound 13 was observed as the most potent inhibitor of AChE with a Kİ value of 0.94 ± 0.13 µM (all compound Kİ values between 0.94 ± 0.13 and 4.47 ± 0.92), also this compound was observed as the most potent inhibitor of BChE with a Kİ value of 0.82 ± 0.11 µM (all compounds had Kİ values between of 0.82 ± 0.11 and 3.48 ± 0.92). Almost all compounds were shown better inhibition profile than standard compound. In the theoretical calculations, the comparison of the biological activities of isatin-thiosemicarbazone hybrid derivatives against enzymes was studied. The enzymes studied in docking calculations are AChE and BChE. Then, ADME/T analysis was conducted to examine the drug properties of these derivatives. Besides, the antimicrobial activity of these molecules was investigated by the microdilution method according to Clinical Laboratory Standards Institute (CLSI) criteria in the study. Cytotoxic activity of isatin-thiosemicarbazone hybrids was determined by the XTT cell viability assay on human breast cancer cell lines MCF-7 and MDA-MB-231. Among the hybrid compounds, compound 8 exhibited the most potent cytotoxic activity with IC50 values of 23.42 ± 0.21 µg/mL and 19.68 ± 0.23 µg/mL on MCF-7 and MDA-MB-231 cell lines, respectively. Overall, the hybridization of isatin and thiosemicarbazone skeleton has played an essential role in the inhibition of enzymes and cytotoxic activity.

Anahtar Kelimeler

Science Direct

BM Sürdürülebilir Kalkınma Amaçları

Atıf Sayıları
Scopus	36

Determination of biological studies and molecular docking calculations of isatin-thiosemicarbazone hybrid compounds

Dergi Adı	Journal of Molecular Structure
Kısa Adı	J MOL STRUCT
Yayıncı	ELSEVIER
Açık Erişim	Hayır
ISSN	0022-2860
E-ISSN	1872-8014
Wos Quartile	Q2
Scopus Quartile	Q2
Tarandığı Indeksler	SCIE , Scopus
WoS Kategoriler	CHEMISTRY, PHYSICAL
Scopus Kategoriler	ANALYTICAL CHEMISTRY \| INORGANIC CHEMISTRY \| ORGANIC CHEMISTRY \| SPECTROSCOPY

Determination of biological studies and molecular docking calculations of isatin-thiosemicarbazone hybrid compounds

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