Evaluation of anticancer effects by different fragments of amyloid-β on non-small cell lung cancer cells | Poster Board #384

Alzheimer’s disease (AD), a neurodegenerative disorder, and cancer, a disease that occurs as a result of abnormal cell division, are two of the leading causes of death globally. Recently, these two diseases have been reported to share several key pathophysiological features and an inverse relationship between them exists; patients suffering from AD have some protection against developing tumors and a low chance of developing cancer. On the other hand, patients who have been diagnosed with cancer show a slower cognitive decline and are less likely to develop AD. Amyloid-β (Aβ), a 1-40/42 amino acid residue peptide that is generated as a result of the cleavage of the amyloid precursor protein, is likely partially responsible for this inverse relationship. The hydrophobic nature of the Aβ protein allows it to self-aggregate to form plaques in the brain of patients with AD, and this same oligomerization is detrimental to cancer cells. In addition, Aβ contains binding regions for acetylcholinesterase at residues 1-16 and 12-28. Previously, we reported that different fragments of Aβ along with the full length peptide, reduced the level of acetylcholine, which is known to enhance the growth of cancer cells, by increasing the activity of acetylcholinesterase in A549 lung cancer cells. In this study, the anticancer activities of several fragments, including 1-16, 1-28, 12-28, and 25-35, all synthesized by solid phase peptide synthesis, will be evaluated using an MTT assay and the IC50s of the peptide fragments will be reported.