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Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study

Journal of Biomolecular Structure and Dynamics · Ocak 2024

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YÖKSİS Kayıtları
Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study
Journal of Biomolecular Structure and Dynamics · 2023 SCI-Expanded
Doç. Dr. HANİF ŞİRİNZADE →
YÖKSİS ISSN Eşleşmesi

Bu dergide (ISSN eşleşmesi) kurumun 7 kaydı bulundu.

YÖKSİS Kayıtları — ISSN Eşleşmesi
Biologically active compounds from two members of the Asteraceae family:Tragopogon dubius Scop. and Tussilago farfara L.
2018 ISSN: 0739-1102 SCI-Expanded
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Formation of the Inclusion Complex of Water Soluble Fluorescent Calix[4]arene and Naringenin: Solubility, Cytotoxic effect and Molecular Modeling Studies
2019 ISSN: 0739-1102 SCI
Prof. Dr. MUSTAFA YILMAZ →
Biologically active compounds from two members of the Asteraceae family: Tragopogon dubius Scop. and Tussilago farfara L.
2019 ISSN: 0739-1102 SCI
Prof. Dr. GÖKHAN ZENGİN →
Formation of the inclusion complex of water soluble fluorescent calix[4]arene and naringenin: solubility, cytotoxic effect and molecular modeling studies
2020 ISSN: 0739-1102 SCI-Expanded Q2
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Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study
2023 ISSN: 0739-1102 SCI-Expanded Q3
Doç. Dr. HANİF ŞİRİNZADE →
Water-soluble Pillar[5]arene-based drug candidates for lung and breast cancer
2025 ISSN: 0739-1102 SCI-Expanded Q1
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Development of a novel apigenin prodrug programmed for alkaline-phosphatase instructed self-inhibition to combat cancer
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Makale Bilgileri

ISSN07391102
Yayın TarihiOcak 2024
Cilt / Sayfa42 · 12011-12020
Özet In this study, the in vitro effects of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II were investigated. A series of N-methylindole hydrazide/hydrazone derivatives (1a-1t) were tested on these enzymes. The interactions of the synthesized indole derivatives with target enzymes were studied by molecular docking methodology. The results revealed that indole derivative Schiff base compounds inhibited the enzymes significantly. Ki values for hCAI isoenzyme were determined to be in the range of 36.18 ± 3.07–224.29 ± 5.78 nM; for the hCAII isoenzyme in the range of 31.30 ± 2.63–201.64 ± 7.25 nM; for acetylcholinesterase in the range of 6.82 ± 0.72–110.30 ± 9.26 nM. Compared to the control compound Acetazolamide (AZA), 1k and 1p were found to have the best inhibitory effect for hCAI; 1p was found to be the best inhibitory effect for hCAII. Compared to the control compound Tacrine (TAC), 1s showed the best inhibitory effect for AChE. In vitro results were verified with the results obtained by docking studies and interactions with enzymes were demonstrated. Communicated by Ramaswamy H. Sarma.

Yazarlar (5)

1
Ebru Akman
2
Hanif Şirinzade
3
Serap Yilmaz Ozguven
4
Esra Dilek
5
Sibel Süzen

Anahtar Kelimeler

Acetylcholinesterase enzyme inhibition human carbonic anhydrase isoforms I and II indole schiff bases molecular docking

Kurumlar

Ankara Üniversitesi
Ankara Turkey
Erzincan Binali Yıldırım Üniversitesi
Erzincan Turkey
Selçuk Üniversitesi
Selçuklu Turkey
Trakya Üniversitesi
Edirne Turkey
Scimago Dergi (ISSN Eşleşmesi)
Journal of Biomolecular Structure and Dynamics
Q2
SJR Skoru0,533
H-Index98
YayıncıTaylor and Francis Ltd.
ÜlkeUnited Kingdom
Medicine (miscellaneous) (Q2)
Molecular Biology (Q3)
Structural Biology (Q3)
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Metrikler

8
Atıf
5
Yazar
5
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