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Jan 21, 2025Keywords:
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Main Article Content
In silico evaluation of verbenone and selected solubilizing compounds against diabetes-related proteins
Abstract
Verbenone is a colourless, minty liquid that is soluble in non-polar solvents with in vitro and in vivo antidiabetic activities. This study evaluates verbenone and selected solubilizing compounds in silico against diabetes related proteins which included glucokinase (1V4S), human pancreatic α-amylase (1B2Y), and sucrase-isomaltase (3AXH). The structures of verbenone, acarbose, and five identified solubilizing compounds were downloaded in SDF format from the PubChem database. The binding energies were computed using Autodock Vina software while physicochemical properties and ADME parameters were predicted using SwissADME server. In glucokinase and human pancreatic α-amylase, the binding affinity (Kcal/mol) of verbenone (-5.4, -5.9) was superior to lysine (-4.5, -
4.7) and eudragit (-4.5, -3.6), while in sucrase-isomaltase, the binding affinity (Kcal/mol) of verbenone (-6.1) was superior to lysine (-5.2), cyclodextrin (-4.8) and eudragit (-4.0) respectively. Only cyclodextrin violated the Lipinski rule of five. More so, cyclodextrin, lysine and eudragit are very soluble, with low lipophilicity compared with verbenone. Lysine and eudragit possess high gastrointestinal absorption and are not suitable P-gp substrate, while eudragit can effectively cross blood brain barrier. The study identified cyclodextrin, lysine and eudragit as potent candidates to improve the bioactivity of verbenone, as alternate means to improve the antidiabetic activity of verbenone.
