DNA protection, molecular docking, antioxidant, antibacterial, enzyme inhibition, and enzyme kinetic studies for parietin, isolated from Xanthoria parietina (L.) Th. Fr.

Abstract

Parietin was isolated from Xanthoria parietina (L.) Th. Fr.’ (methanol:chloroform) extract, using a silica column. 13 C NMR and 1H NMR were used to confirm the structure of the isolated parietin. For the first time, parietin was investigated for its antioxidant, antibacterial and DNA protective activities. Molecular docking was carried out to determine the binding affinity and interactions between the enzymes and our molecule. Inhibition and kinetic mechanism studies for the action of the enzymes were performed too. Parietin exhibited high metal chelating activity. The MIC values of parietin were sufficient to inhibit different bacterial strains; E. coli, P. aeruginosa, K. pneumoniae and S. aureus. Molecular docking applications exhibited that acetylcholinesterase (AChE), butyrylcholinesterase (BChE), lipase, and tyrosinase have high potential for binding with the parietin. Especially, the parietin’s highest binding affinity was recorded with AChE and tyrosinase. These results were confirmed by the inhibition and kinetics results, where, parietin observed a potent inhibition with an IC₅₀ values between 0.013-0.003 µM. Moreover, parietin acts’ as a non-competitive inhibitor against AChE, BChE, and lipase, and as a competitive inhibitor against tyrosinase with a high rate of inhibition stability. The promising biological properties of parietin revealed its effectiveness in terms of suitability in the food and pharmaceutical industries.

Communicated by Ramaswamy H. Sarma

Keywords:

• Xanthoria parietina
• parietin
• antioxidant
• antimicrobial
• DNA protective
• enzyme inhibition
• kinetic mechanism
• molecular docking

Disclosure statement

No potential conflict of interest was reported by the authors.

Additional information

Funding

The study funded by Scientific Research Project, Ondokuz Mayis University, Samsun-Turkey (OMU-BAP), under grant numbers (PYO.FEN.1904.19.006 and PYO.FEN.1904.20.002).