Phytochemical Analysis and Screening of Acetylcholinesterase and Carbonic Anhydrase I and II Isoenzymes Inhibitory Effect of Heptaptera triquetra (Vent.) Tutin Root
Yazarlar (8)
Ayşe Çi̇Çek Kaya
Atatürk Üniversitesi, Türkiye
Prof. Dr. Hilal Özbek Atatürk Üniversitesi, Türkiye
Doç. Dr. Hafize Yuca Atatürk Üniversitesi, Türkiye
Doç. Dr. Gülderen YILMAZ Ankara Üniversitesi, Türkiye
Dr. Öğr. Üyesi Zeynebe BİNGÖL Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Prof. Dr. Cavit Kazaz Atatürk Üniversitesi, Türkiye
Prof. Dr. İlhami Gülçin Atatürk Üniversitesi, Türkiye
Prof. Dr. Zühal Güvenalp Atatürk Üniversitesi, Türkiye
Makale Türü Açık Erişim Diğer (Teknik, not, yorum, vaka takdimi, editöre mektup, özet, kitap krıtiği, araştırma notu, bilirkişi raporu ve benzeri) (Diğer hakemli uluslararası dergilerde yayınlanan teknik not, editöre mektup, tartışma, vaka takdimi ve özet türünden makale)
Dergi Adı Fabad Journal of Pharmaceutical Sciences
Dergi ISSN 1300-4182 Scopus Dergi
Dergi Tarandığı Indeksler TR DİZİN
Makale Dili Türkçe Basım Tarihi 10-2022
Cilt / Sayı / Sayfa 47 / 3 / 381–392 DOI 10.55262/fabadeczacilik.1147174
UAK Araştırma Alanları
Farmasotik Botanik
Özet
Alzheimer’s disease (AD) is characterized by progressive memory loss, deterioration of other cognitive functions, and inability to perform activities of daily living. Inhibiting the acetylcholinesterase (AChE) enzyme causes Ach accumulation in cholinergic synapses. This situation is expected to increase cognitive functions. Carbonic anhydrase enzymes (CAs) are ubiquitous in all living organisms. They have crucial physiological and pathological roles. CA inhibitors (CAIs) bind to catalytic zinc ions in the active site of CA isoenzymes and block their activity. The clinical use of CAIs had been established as antiglaucoma, anticonvulsant agents, diuretics, and anti-obesity drugs, in managing mountain sickness, gastric and duodenal ulcers, neurological disorders, osteoporosis, and tumors. To evaluate the bioactive profile of Heptaptera triquetra root, isolation studies, AChE, and human carbonic anhydrase (hCA) I and II inhibitory activities were performed. According to isolation studies, one fatty acid, coniferyl palmitate (1); four sesquiterpene coumarins, umbelliprenin (2), badrakemin acetate (4), colladonin (5), karatavicinol (6); and two sterols, stigmasterol (3a), β-sitosterol (3b) were isolated. All isolated compounds showed high potency against all enzymes (except badrakemin acetate for AChE) compared to standards. Umbelliprenin (2) with an IC50 value of 31.500 nM against hCA I, colladonin (5) with an IC50 value of 36.473 nM against hCA II and stigmasterol (3a), and β-sitosterol (3b) mixture with an IC50 value 9.000 nM against AChE demonstrated the best activity.
Anahtar Kelimeler
acetylcholinesterase | Apiaceae | carbonic anhydrase | enzyme inhibition | Heptaptera triquetra | isolation