Plectrabarbene, a New Abietane Diterpene from Plectranthus barbatus Aerial Parts

• Published in: Molecules (Basel, Switzerland) Vol. 25; no. 10; p. 2365
• Main Authors: Musayeib, Nawal M Al, Amina, Musarat, Al-Hamoud, Gadah Abdulaziz, Mohamed, Gamal A, Ibrahim, Sabrin R M, Shabana, Samah
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 20.05.2020; MDPI
• Subjects: abietane diterpene; Abietanes - chemistry; Abietanes - isolation & purification; acetylcholinesterase inhibition; Amino acids; Bioassays; Carbon; Cholinesterase Inhibitors - chemistry; Cholinesterase Inhibitors - isolation & purification; Diterpenes; Diterpenes - chemistry; Diterpenes - isolation & purification; Donepezil; Flavonoids; Humans; Hydrogen bonds; Labiatae; Ligands; Medical research; Molecular docking; Molecular Docking Simulation; Molecular Structure; Oils & fats; Pharmaceutical industry; Plant Components, Aerial - chemistry; Plant Extracts - chemistry; plectrabarbene; Plectranthus - chemistry; Plectranthus barbatus; Brazil; Africa; Plectranthus barbatus; acetylcholinesterase inhibition; plectrabarbene; abietane diterpene; molecular docking; Labiatae
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules25102365

A new abietane diterpene namely plectrabarbene ( ), together with two known compounds: sugiol ( ) and 11,14-dihydroxy-8,11,13-abietatrien-7-one ( ) have been isolated from the aerial parts of Andr. (Labiatae). The structures of these compounds were determined by various spectral techniques (e.g., UV, IR, NMR, and FAB) and by comparison with the literature data. A molecular docking study of the isolated diterpenes ( - ) was performed with AChE to gain an insight into their AChE inhibition mechanism. The results of docking experiments revealed that the all tested compounds showed binding affinity at the active site of AchE in comparison to donepezil.