A IN2UB study featured in the cover of ChemPhysChem

Diseases such as Alzheimer’s and Parkinson’s and others like cataracts are known for the uncontrolled protein aggregation. A study led by researchers from the Institute of Nanoscience and Nanotechnology of the UB (IN2UB) identified the general features of a protein aggregation when its concentration varies. The study has been featured in the cover of the journal ChemPhysChem in their March issue.

When proteins' concentration is below a specific value, these fold spontaneously in bio-origami shapes -their native structures- without noticing the presence of other proteins. This enables the cell that has them to function with the series of biomolecules that build it. If this concentration exceeds due to an anomaly, proteins unfold and, in general, their biological function stops. This is the previous step to their aggregation, which occurs if the concentration continues to exceed.

According to Giancarlo Franzese, researcher at IN2UB and member of the Section of Statistical Physics and Interdisciplinary Physics of the Department of Condensed Matter Physics, “the study concludes there is a range of concentrations in which we can act, for instance, with drugs that block the aggregation so as to fight the disease. Another strategy could be to seek drugs to lower the protein concentration to prevent aggregation”.

This result responds to the science debate on whether the two phenomena -loss of native state and aggregation- happen at the same time. In addition, “the study shows the fundamental role of water structural fluctuations in these phenomena, since it hydrates proteins and is the base to explain the change in protein behaviour”, concludes Franzese.

The study was carried out in collaboration with researchers from CIC biomaGune (Basque Country) and the Complutense University of Madrid.

Article reference:

V. Bianco, G. Franzese and I. Coluzza. "In Silico Evidence That Protein Unfolding is a Precursor of Protein Aggregation". ChemPhysChem. March 2020. DOI: https://doi.org/10.1002/cphc.20200009