ProtEprobe takes advantage of the recent cutting edge developments in protein conformation control at the Malliaras group and high sensitive protein sensing using high sensitivity factor triangular silver nanoplates by the fellow. Misfolding of a protein occurs when 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 distinctly alter protein secondary structures. Proteins associated with protein misfolding diseases, incuding neurodegenerative diseases such as Alzheimer's, undergo conformational changes such as the transformation of largely random coiled or α-helix structures to the highly ordered β-structures found in protein fibrils. Amyloid fibrils formed from peptide Amyloid beta (Aβ), are a major component of amyloid plaques in the brains of Alzheimer’s patients. The ProtEprobe technique will use electrical potential gradients to stimulate and control the conformation transitions of proteins including the cell adhesion protein Fibronectin and Aβ on 3D electrospun conductive polymer tissue scaffolds. The high sensitive spectral response of the nanoplate monitors will be used to analyse protein conformational transitions and observe the progression of Aβ fibril formation. Investigations will be carried out to ascertain the impact of the presence of an electric field and the capacity to tune the strength in order to enable improved understanding and selection of protein conformations on tissue scaffolds, towards enhancing cell surface interactions, healing of misfolding and facilitating the restoration of the structure and function of diseased tissues. In a paradigm step towards imparting a new dimension to tissue regeneration, ProtEprobe will develop 3D bioactive scaffolds with electrically programmable protein conformation and in situ real-time protein nanomonitors paving the way for the treatment and prevention of many neurodegenerative diseases.