A novel technique to characterize conformational state of the proteins: p53 analysis

As the technology is advancing, biotechnologist and pharmacologist seems more interested and focused towards the development of innovative sensing solution/technology capable of evaluating proteins without any limitations of time and cost which were encountered/offered by conventional/traditional methods such as ELISA used for protein quantification. To allow continuous monitoring and attain protein sample information in a non-invasive way, spectrophotometry might be considered as an alternate method which analyzes different conformational states of proteins by closely observing the variation in optical properties of the sample. The work presented studies p53 protein conformational dynamics and their involvement in various pathophysiological and neurodegenerative disease/disorders using the spectrophotometer-based method. By utilizing the technique of spectrophotometry, investigations were carried out on three samples containing varied molecular state of p53 (Wild p53, Denatured p53, and Oxidized p53), to detect the difference in light absorption. Overall, this proposes the possibility of a simple, non-invasive and optical based method capable of detecting and identifying different structural states of p53 while overcoming the complexities offered by the conventional procedures.