Exploring tryptamine derivatives as potential agents for diabetes and cancer treatment: <i>in-vitro</i> kinetics, molecular docking, and cell toxicity based investigations
Abnormal glucose levels in diabetes mellitus cause chronic complications like neuropathy, nephropathy, retinopathy, cataract, and cardiovascular issues. Aldose reductase (AR), an enzyme in the polyol pathway, is crucial for developing treatments for diabetic complications. To this end, a series of twenty inhibitors based on tryptamine scaffolds were synthesized and assessed for their efficacy in inhibiting AR activity. The compounds showed strong to moderate inhibition of AR with IC<sub>50</sub> values ranging from 0.07 µM to 8.11 µM. Among these analogs, <b>3</b> showed the highest IC<sub>50</sub> value (0.07 ± 0.9 µM), and <b>1</b> showed the weakest inhibition of AR (IC<sub>50</sub> = 8.11 ± 0.7 µM). Furthermore, the cytotoxic potential of these analogs was tested in human fibroblast cells (BJ cell line), where all the compounds showed no toxic effect. Having the advantage of the non-toxic factor of the compounds, these molecules were further tested for anti-cancerous activity in glioblastoma multiforme (GBM) cell line U87. Compounds <b>1-5</b>, <b>14</b>, <b>17</b>, and <b>20</b> showed significant inhibitory effects on the growth of U87 cells in various concentrations, whereas compounds <b>6</b>, <b>11</b> and <b>18</b> showed moderate inhibition. <i>In-vitro</i> mechanistic studies show that compounds have competitive mode of inhibition for AR. Furthermore, molecular docking studies reveal that these compounds fit appropriately into the active site of AR. Finally, our study explores the stability and binding affinities of selected tryptamine-based inhibitors of AR using molecular dynamics simulations, identifying compounds <b>2</b> and <b>3</b> as promising candidates for therapeutic development.
Publication Details
- Journal
- Figshare
- Published
- 2025-01-01
- DOI
- https://doi.org/10.6084/m9.figshare.29313077
- Primary Topic
- Aldose Reductase and Taurine
- Type
- article
- Field-Weighted Citation Impact
- 0.00