Phytochemical analysis of Robinia pseudoacacia flowers and leaf: quantitative analysis of natural compounds and molecular docking application
Yazarlar (3)
Prof. Dr. Ramazan ERENLER Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale (Diğer hakemli uluslarası dergilerde yayınlanan tam makale)
Dergi Adı Turkish Journal of Biodiversity
Dergi ISSN 2667-4386
Dergi Tarandığı Indeksler Scientific Indexing Services (SIS)
Makale Dili İngilizce Basım Tarihi 01-2024
Kabul Tarihi 02-04-2024 Yayınlanma Tarihi 30-06-2024
Cilt / Sayı / Sayfa 7 / 1 / 1–10 DOI 10.38059/biodiversity.1446241
Makale Linki https://turkbiod.artvin.edu.tr/en/
UAK Araştırma Alanları
Organik Kimya
Özet
Phenolic compounds are widely found and well-known secondary metabolites in plants. Identification, and quantification of phenolic compounds, and determination of their biological activities reveal the unknown secrets of plants. Robinia pseudoacacia (RP) is known as the white-flowered false acacia and is distributed in Northern Anatolia in Turkey. Spectrophotometric and chromatographic techniques are used to identify the presence and amount of phenolics. In this study, RP flowers and leaves were extracted with methanol and analyzed by LC-MS/MS to determine their phytochemical content. Salicylic acid and syringic acid were found as major products in leaves and flowers. RP extracts have been reported to have antibacterial activity and BChE inhibitory properties. Therefore, the BChE and DD peptidase enzyme inhibitory properties of the main components salicylic acid and syringic acid were investigated by molecule docking (MolDock). According to MolDock results, syringic acid interacted with BChE and DD peptidase and was calculated as a MolDock score of -79.38, and -71.25, with binding energies -5.90, and -5.40 kcal/mol respectively. Salicylic acid interacted with BChE and DD peptidase and was calculated as a MolDock score of -63.54, and -66.18, with binding energies of -6.10, and -5.70 kcal/mol respectively. As a result, salicylic acid had higher binding energy in its interactions with BChE and DD peptidase enzymes. In theory, salicylic acid can be used as a good BChE and DD peptidase inhibitor.
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