Publication details
Fast and sensitive electrochemical detection of native, denatured, and aggregated forms of tumor supressor protein p53
| Authors | |
|---|---|
| Year of publication | 2004 |
| Type | Article in Proceedings |
| Conference | Molecular Biology of the Cell |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | protein p53; electrochemical detection; structural forms; aggregation; denaturation |
| Description | Protein p53 is a transcriptional factor, which is routinely attendant in a cell at low concentrations. Alzheimer's disease, Parkinson's disease, cystic fibrosis, prion diseases, and many types of cancer are considered to be protein p53 conformation diseases. Most of them are also known as amyloidogenic diseases due to the occurrence of pathological accumulation of insoluble aggregates with fibrillar conformation. Some neuroblastomas, carcinomas, and myelomas show an abnormal accumulation of the wild-type tumor suppressor protein p53 either in the cytoplasm or in the nucleus of the cell. Electrochemical methods could be a suitable tool for study of very low protein p53 intracellular concentrations. In our work, protein p53 was analyzed by flow injection analysis coupled with electrochemical detector. The optimized method was rapid (less then five minutes) and sensitive (protein p53 detection limit was 45 amol). The sensitive detection method was applied to the study structural changes of protein p53 (denaturation and aggregation). Considerable changes in electrochemical responses of individual protein p53 forms were observed. That is why the denatured and aggregated protein p53 form could be easily differentiated from the native form of protein p53. The described method brings a new effective tool for the study of normal and tumorous cells. |