Abstract
Organic selenium shows promise in cancer treatment due to its antioxidant properties, however, challenges like toxicity and instability hinder its efficacy. Herein, we aim to develop stable and less toxic selenium-chelated tuna bone gelatin peptides (TBGP@Se). TBGPs were extracted from tuna bones and chelated with selenium through a redox reaction. The resulting TBGP@Se was characterized to assess amino acids sequences, morphology of TBGP@Se, particle size distribution. Antiproliferation activity was evaluated using A549 and HT-29 cell lines. Our TBGP@Se was rich in glycine, proline, and alanine which aided stable Se chelation. Electron micrography confirmed gelatin concentrations (5 mg mL(-1)) with stable TBGP@Se complexes. FTIR and DLS analyses further confirmed successful Se chelation and improved particle dispersion. TBGP@Se exhibited potent antiproliferative effects in vitro. Collectively, our study demonstrates the successful synthesis of stable TBGP@Se with significant antiproliferative activity against cancer cells in vitro. Future research should explore the mechanisms of action and validate these findings in animal models to advance TBGP@Se towards clinical applications in cancer treatment.