(−)-Kusunokinin as a Potential Aldose Reductase Inhibitor: Equivalency Observed via AKR1B1 Dynamics Simulation
Tanotnon Tanawattanasuntorn, Tienthong Thongpanchang, Thanyada Rungrotmongkol, Chonnikan Hanpaibool, Potchanapond Graidist, Varomyalin Tipmanee
Abstract
), as well as a similar interactive insight of the enzyme pocket, pinpointed an ARI equivalence of (-)-kusunokinin. An aromatic ring and a γ-butyrolactone ring shared a role with structural counterparts in known inhibitors. The modeling explained that the aromatic constituent contributed to π-π attraction with Trp111. In addition, the γ-butyrolactone ring bound the catalytic His110 using hydrogen bonds, which could lead to enzymatic inhibition as a consequence of substrate competitiveness. Our computer-based findings suggested that the potential of (-)-kusunokinin could be furthered by in vitro and/or in vivo experiments to consolidate (-)-kusunokinin as a new AKR1B1 antagonist in the future.