Cancer is a deadly disease that has claimed millions of lives worldwide. Traditional cancer treatments, such as chemotherapy and radiation, have been used for many years but have become less favored due to drug resistance, lack of tumor selectivity, high costs, and various side effects, such as fatigue and hair loss. Many studies have reported that animal venoms, such as those from snakes, scorpions, and bees, contain bioactive peptides that can be synthesized into anti-- cancer peptides (ACPs), which offer a potential alternative to traditional cancer therapies. Apitherapy is an area of growing interest for the development of new cancer treatments using bee venom, which is a complex mixture of biologically active peptides, enzymes, bioactive amines, and nonpeptide components that have been found to have anti-cancer properties. By leveraging these bioactive peptides, researchers could develop ACPs that are more targeted towards cancer cells, reducing the risk of adverse side effects and improving patient outcomes. The use of bee venom components in targeting cancer could provide a more selective, effective, and affordable approach to cancer therapy. While further research is needed, the potential benefits of using bee venom components in cancer therapy are significant and could help improve the lives of cancer patients worldwide. This study aims to review the components of bee venom as potential cancer treatments.
Diabetes, particularly type II, is a global health concern, with current treatments like α-glucosidase inhibitors often causing gastrointestinal side effects. This study explored the antihyperglycemic potential of crude protein hydrolysate from oil palm leaves (OPL) as a plant-based α-glucosidase inhibitor. OPL protein hydrolysate was extracted under acidic, neutral, and alkaline conditions, and their α-glucosidase inhibitory activity was assessed. OPL hydrolysate obtained under neutral conditions for 2 h showed the highest inhibitory activity, comparable to the standard drug, acarbose. Bioassay-guided fractionation of the most potent extract revealed that peptides from sub-fractions C1 and C9 exhibited stronger inhibition, with IC50 values of 66.3 and 62.0 μg/mL, respectively. Seven novel peptides were identified from these fractions, and molecular docking confirmed stable interactions between these peptides and the α-glucosidase enzyme via hydrogen bonds and salt bridges. These findings suggest that OPL protein hydrolysate is a plant-based promising natural α-glucosidase inhibitor with potential as an antidiabetic agent. Future studies should focus on in vivo validation of its efficacy and safety for therapeutic use.