Professor Michele Vendruscolo is studying the principles by which the amino acid sequences of proteins determine a wide range of properties beyond their native structures and their ability to fold.
He has shown that the physico-chemical properties of protein sequences can be used to rationalise and predict the abundance of proteins within cells, and the nature of their interactions with other cellular components, ranging from functional partners to protective species such as molecular chaperones.
This approach has generated rational design procedures for the modification of protein behaviour, thus suggesting therapeutic approaches directed at many types of disease, including those involving the disordered proteins associated with neurodegenerative conditions such as Alzheimer’s and Parkinson’s diseases.
In particular, by enabling proteome-wide analyses of the factors regulating protein homeostasis, his methods are offering new insights into the manner in which physics and chemistry regulate the biochemical reactions taking place in living organisms, and have led him to clarify the fundamental role that protein solubility has in the maintenance of protein homeostasis.
He has recently demonstrated how these approaches are able to provide a rational basis for diagnostic and therapeutic strategies to combat some of the most prevalent and still incurable diseases.