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Journals / International Journal of Secondary Metabolite / 2026 / Volume: 11 Issue: 1

Inhibition of carbonic anhydrase and cholinesterase enzymes by acetone extract of Bryoria capillaris (Ach.) Brodo & D.Hawksw.

Yalçın Karagöz(AĞRI İBRAHİM ÇEÇEN ÜNİVERSİTESİ, ECZACILIK FAKÜLTESİ)0000-0002-4835-4508
Naim Uzun(AGRI IBRAHIM CECEN UNIVERSITY, FACULTY OF PHARMACY)0000-0002-9763-7643
Bayram Alparslan(AGRI IBRAHIM CECEN UNIVERSITY, FACULTY OF PHARMACY)0000-0001-6973-7455
Murat Şentürk(AGRI IBRAHIM CECEN UNIVERSITY, FACULTY OF PHARMACY)0000-0002-9638-2896
Pages
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Publication Date
2024-02-05
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

These results indicate that BC extract has a high potential to provide new drug candidates for all the tested enzymes, particularly for BChE.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:In traditional medicine, people commonly consume Bryoria capillaris (BC) as flour and tea, particularly in Northeast Anatolia, where it is one of the most prevalent lichen species.
📊
Key Findings & Data:We determined IC50 values of BC for each enzyme to measure the level of inhibition.
💡
Conclusion & Impact:These results indicate that BC extract has a high potential to provide new drug candidates for all the tested enzymes, particularly for BChE.
🔬Design:Research Article
📍Scope:Comprehensive Sample
⚙️Variables:Lichen · Enzyme · Bryoria capillaris

Abstract

In traditional medicine, people commonly consume Bryoria capillaris (BC) as flour and tea, particularly in Northeast Anatolia, where it is one of the most prevalent lichen species. This study aimed to obtain an acetone extract of BC and investigate its inhibitory effects on carbonic anhydrase (CA) I, CA II, acetylcholine esterase (AChE), and butyrylcholine esterase (BChE) enzymes. We determined IC50 values of BC for each enzyme to measure the level of inhibition. The IC50 values for CA I and CA II were 8.77 μg/mL and 7.56 μg/mL, respectively. Acetazolamide, a specific CA I and II inhibitor, had IC50 values of 1.65 and 0.016 μg/mL, respectively. The IC50 values of BC for AChE and BChE were 7.96 and 8.58 μg/mL, respectively. Galantamine had IC50 values of 4.68 and 16.07 μg/mL for AChE and BChE, respectively. These results indicate that BC extract has a high potential to provide new drug candidates for all the tested enzymes, particularly for BChE.

Özet

In traditional medicine, people commonly consume Bryoria capillaris (BC) as flour and tea, particularly in Northeast Anatolia, where it is one of the most prevalent lichen species. This study aimed to obtain an acetone extract of BC and investigate its inhibitory effects on carbonic anhydrase (CA) I, CA II, acetylcholine esterase (AChE), and butyrylcholine esterase (BChE) enzymes. We determined IC50 values of BC for each enzyme to measure the level of inhibition. The IC50 values for CA I and CA II were 8.77 μg/mL and 7.56 μg/mL, respectively. Acetazolamide, a specific CA I and II inhibitor, had IC50 values of 1.65 and 0.016 μg/mL, respectively. The IC50 values of BC for AChE and BChE were 7.96 and 8.58 μg/mL, respectively. Galantamine had IC50 values of 4.68 and 16.07 μg/mL for AChE and BChE, respectively. These results indicate that BC extract has a high potential to provide new drug candidates for all the tested enzymes, particularly for BChE.

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Cite This Article

Karagöz, Y., Uzun, N., Alparslan, B., Şentürk, M. (2024). Inhibition of carbonic anhydrase and cholinesterase enzymes by acetone extract of Bryoria capillaris (Ach.) Brodo & D.Hawksw.. International Journal of Secondary Metabolite, Volume: 11 Issue: 1. https://doi.org/10.21448/ijsm.1368533

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