Enzyme Inhibition Properties and Molecular Docking Studies of 4-Sulfonate Containing Aryl α-Hydroxyphosphonates Based Hybrid Molecules
Yazarlar (7)
İrfan Şahin
Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
Dr. Öğr. Üyesi Zeynebe BİNGÖL Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Sultan Onur
Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
Seyit Ali Güngör Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
Muhammet Köse Kahramanmaraş Sütçü İmam Üniversitesi, Türkiye
İlhami Gülçin Atatürk Üniversitesi, Türkiye
Ferhan Tümer Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Chemistry and Biodiversity (Q3) | ||
| Dergi ISSN | 1612-1872 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | Türkçe | Basım Tarihi | 01-2022 |
| Cilt / Sayı / Sayfa | 19 / 5 / – | DOI | 10.1002/cbdv.202100787 |
| Makale Linki | http://dx.doi.org/10.1002/cbdv.202100787 | ||
| Özet |
| In this study, a series of new hybrid molecules containing two important functional groups on the same skeleton were designed. 4-Hydroxybenzaldehyde and its two different derivatives were converted into their respective sulphonates by interacting with tosylchloride and methanesulfonyl chloride. Then, the desired molecules were synthesized by adding diethoxyphosphonate to the aldehyde group. Also, novel synthesis of hybrid compounds (4a–c and 5a–c) were tested toward some metabolic enzymes like carbonic anhydrase I and II isoenzymes (hCA I and hCA II) and acetylcholinesterase (AChE) enzyme. The synthesis of hybrid compounds (4a–c and 5a–c) showed Ki values of in range of 25.084±4.73-69.853±15.19 nM against hCA I, 32.325±1.67–82.761±22.73 nM against hCA II and 1.699±0.25 and 3.500±0.91 nM against AChE. For these compounds, compound 4c showed maximum inhibition effect against hCA I and hCA II isoenzymes and compound 5b showed maximum inhibition effect against AChE enzyme. By performing docking studies of the most active compounds for their binding modes and interactions were determined. |
| Anahtar Kelimeler |
| acetylcholinesterase | carbonic anhydrase | enzyme inhibition | molecular docking studies | α-hydroxy phosphonates |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| WoS | 17 |
| SCOPUS | 19 |
| Google Scholar | 20 |