| 초록 |
The p53 protein is a well-known tumor suppressor that plays an important role in preventing cancer. The mutations of p53 such as functional damage of its DNA binding domain lead to tumors. Specially, the mutants of p53 at hot spot have unique changes of local electron density that affect specificity of DNA binding compared with the wild types. This can be detected by Rayleigh light scattering according to the changes of localized surface plasmon resonance (LSPR). The LSPR Δλmax shift of mutant p53 proteins is significantly lower than that of wild types. These differences propose that hot-spot mutants can be easily detected by local electron density alterations that disturbs the specificity of DNA binding domain of p53 on the nanoplasmonic sensor. By this strategy, the nanoplasmonic sensor can detect mutant p53 proteins from wild types of real samples simply and directly, facilitating the efficient screening of many mutant proteins. |
