In Vitro and In Silico Assessment of Bioactivity Potencies With Components of Aristolochia bodamae Dingler Extracts From Turkey

• Published in: ChemistrySelect (Weinheim) 2024-11, Vol.9 (43), p.n/a
• Main Authors: Ozen, Tevfik, Demir, Merve, Marah, Sarmad, Korkmaz, Hasan
• Format: Article
• Language: English
• Subjects: Aristolochia bodamae; Bioactivity; DNA protection activity; Molecular docking; Molecular dynamics; Phytochemicals
• ISSN: 2365-6549; 2365-6549
• DOI: 10.1002/slct.202403703

Aristolochia species have been widely used in folk medicine. In this work, six solvent extracts of Aristoloia bodamae leaf, seed, and flower were investigated for the photochemical contents (TPC, TFC, and LC–MS/MS), bioactivities. Additionally, molecular docking was applied to identify whether the most abundant compounds in the extracts are responsible for the bioactivity. Total phenol and flavonoid content ranges were 10.32–160.54 mg GAE/g and 3.42–50.03 mg QE/g, respectively. The most common chemical found in most extracts was o‐coumaric acid. Leaf extracts showed the highest total antioxidant, reducing power, and free radical removal activities. Seed extracts recorded the highest antibacterial activity, and for the inhibition activity seed extracts were also the highest in general. Molecular docking demonstrates firm binding between o‐coumaric acid and AChE. The stability of the best‐docked protein was evaluated using 100 ns molecular dynamic simulation and an MM‐PBSA‐assisted effective free energy estimation. The results showed that the interaction between this enzyme and the compound was remarkably stable according to energy and molecular dynamics calculations. Overall, aboveground extracts of A. bodamae exhibited high potential in reducing oxidative damage, enzyme inhibition, DNA protection potential, and antibacterial activities, probably due to their phenolic components and o‐coumaric acid. Extracts were in‐vitro tested for antibacterial, antioxidant, DNA protection, and enzyme inhibition activities. In‐silico studies then clarified the role of chemical content, using molecular docking of the o‐coumaric acid with AChE. MD simulations over 100 ns confirmed complex stability and MMPBSA estimations revealed binding energy. Results showed a high‐affinity interaction between o‐coumaric acid and enzyme, forming a relatively stable complex.