Nanosensors for Alzheimer’s diagnosis
To facilitate diagnosis, researchers have generated a new tool for detecting protein conformational activity in living cells.
New and growing evidence reveals a role for protein misfolding in various diseases, including Alzheimer’s.
Physiologically, each protein has a predetermined, three-dimensional structure central to its function. There are cases, however, when proteins misfold into abnormal structures, causing various pathologies.
Alzheimer’s, for example, is caused by the misfolding of the peptide amyloid beta into fibrils and plaques that aggregate in brains. Detection of these misfolded peptides requires a highly sensitive approach to facilitate prompt diagnosis.
Scientists carrying the Seventh Framework Programme (FP7)-funded project ProtEprobe (Electrically Controlled Protein Conformation on 3D Tissue Scaffolds) have set out to develop a technique for detecting protein folding changes.
Using silver nanoplate biosensors to optically detect protein folding and conformation, and organic electrochemical transistors to record changes.
As proof of principle within this technique, the researchers implemented the prototype system for the detection of fibronectin in living cells and serum. The system could discriminate between diffusely bound fibronectin and growing fibrils in an evolving extra cellular matrix.
The ProtEprobe sensor achieved state-of-the-art detection of protein conformation. Its ability to discriminate in this way renders it invaluable for the diagnosis of diseases associated with protein misfolding.
ProtEprobe takes advantage of cutting-edge developments in protein conformation control. Misfolding of a protein occurs after it becomes trapped in a local potential energy minimum where the conformation differs from the native-state structure.
External electric fields have been demonstrated to alter protein secondary structures.
ProtEprobe is funded under FP7’s Marie Skłodowska-Curie Actions pillar.
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