Peptide based Biosensing of Protein Functional Control Indicates Novel Mechanism of Cancerous Development under Oxidative Stress

As a major cause of cancer, oxidative stress simultaneously affects many aspects of protein function. Simultaneous detection of these aspects may provide an overall view of the function of proteins under pathological condition. In this work, employing peptide and amino acid as the probe, a biosensing method is developed to detect proteins, their metal ion cofactors, as well as the cofactor induced protein modification and sub-cellular redistribution. This method enables us to observe, in a colorectal cancer cell line, the oxidative stress induced cotranslocation of p53 and cupric ion into the nuclei, where the Cu induced oxidative modification of p53 may form a nuclear oxidative environment that further leads to oxidative modification and nuclear export of S100A6. The translocation and modification of S100A6 can also be observed in parallel with the progress and invasion of tumor in clinical samples of colorectal cancer. These results confirm the effectiveness of this method as a tool to study the procancerous function of proteins under oxidative and inflammatory condition.

Automated summary

A biosensing method was developed to detect protein function under pathological conditions, showing oxidative stress-induced protein translocation and modification. Clinical samples confirmed the effectiveness of this method in studying the role of proteins in the progression of colorectal cancer.